Engineering heat-stable disease resistance in plants

ABSTRACT

Disclosed are nucleic acid molecules which encode heat-stable plant resistance polypeptides having NB-LRR structural motifs, where the LRR domain includes a sub-domain which confers heat-stability to a plant defense response. The invention further involves transgenic plants and transformed host cells that express these nucleic acid molecules and exhibit enhanced disease resistance over a wide range of temperatures.

STATEMENT AS TO FEDERALLY FUNDED RESEARCH

This work was supported by grant number 2005-35100-16044 from the United States Department of Agriculture. The Government has certain rights in the invention.

BACKGROUND OF THE INVENTION

The invention relates to plant disease resistance.

Plant diseases cause crop losses that are devastating to world food supply and human well being. Plants have evolved defense mechanisms to ward off diverse biotic attacks to ensure their survival and fitness. This plant immunity occurs at multiple levels and can be largely divided into two branches (1, 31). One is a general resistance responding to molecules common to many pathogens and the other is a ‘cultivar-specific’ resistance responding to pathogen virulent factors. The latter resistance is induced upon a specific recognition of the pathogen race-specific avirulence (Avr) gene by the disease resistance (R) gene of the host plant (32). This ‘gene-for-gene’ interaction leads to rapid and efficient defense responses including a form of programmed cell death named hypersensitive response (HR) to restrict the growth of pathogens (33). A number of R genes have been molecularly cloned in many species and the largest class of R proteins contains ‘nucleotide-binding’ (NB) and leucine-rich repeat (LRR) domains (8, 9). A direct or indirect interaction between Avr proteins and the R proteins activates downstream signaling events leading to local HR and systemic acquired resistance throughout plants.

Plant defense responses are modulated by a number of environmental factors including light, humidity, and temperature. Temperature variations influence disease resistance to bacteria, fungi, virus, and insects (34). A high temperature often suppresses disease resistance in plants, and this phenomenon is named ‘heat masking’. This heat sensitivity has been reported in a number of disease resistance responses mediated by R genes such as the N gene in tobacco (35), Mi in tomato (6), RPW8 in Arabidopsis (36), and SNC1 in Arabidopsis (7).

There is accordingly a need in the art for plants having increased sensitivity to temperature thereby avoiding suppression of a resistance response. Disease resistance genes are consequently needed for disease resistance management at high temperatures. The present invention provides such genes and includes methods for conferring disease resistance to plants at temperatures at which defense responses are typically diminished or masked due to heat sensitivity.

SUMMARY OF THE INVENTION

It has been found that temperature modulates plant defense responses through disease resistance proteins. As is described below, through a genetic screen, a temperature sensor in plant disease resistance has been identified, and this sensor is a NB-LRR type of R gene SNC1 from a crucifer, Arabidopsis thaliana. In particular, specific mutant forms of SNC1 have been demonstrated to induce heat-stable disease resistance. Demonstrating the general applicability of this discovery, similar modifications created in another R gene N were also shown to confer heat-stable disease resistance to tobacco mosaic virus. This discovery provides a methodology to engineer or breed plants or both with an ability to mount defense responses over a range of temperatures.

In general, the invention features an isolated nucleic acid molecule which includes a nucleotide sequence encoding a polypeptide including: (a) a nucleotide binding (NB) domain; and (b) a leucine rich repeat (LRR) domain, wherein the LRR domain includes a sub-domain that confers a heat-stable defense response to a plant pathogen. In preferred embodiments, the LRR sub-domain that confers a heat-stable defense response to a plant pathogen includes an E(K or R)LD motif or an E(K or Y)V(N or D) motif.

In other preferred embodiments, the nucleotide sequence is operably linked to a promoter that drives expression in a plant cell. Useful promoters include constitutive promoters, inducible promoters, or a tissue-specific promoter. In preferred embodiments, tissue-specific promoters include root-, leaf-, or seed-specific promoters. Exemplary promoters are described herein. In other preferred embodiments, the isolated nucleic acid molecule is composed, either wholly or partially, of synthetic nucleotide building blocks. In still other preferred embodiments, codon usage of the nucleotide sequence is optimized for expression in a plant.

In preferred embodiments, the expressed polypeptide confers disease resistance on a plant expressing the polypeptide at both 22° C. and 28° C. or at both 22° C. and 30° C. In yet other preferred embodiments, the polypeptide, when expressed in a plant, is localized in the plant cell nucleus.

In other aspects, the invention features a vector, a cell, or a plant which includes any of the aforementioned isolated nucleic acid molecules. Exemplary vectors, cells, and plants are described herein.

In still other aspects, the invention features a method of conferring resistance to a pathogen in a plant, the method includes the steps of: (a) transforming a plant cell with an isolated nucleic acid molecule that encodes a polypeptide which includes: (i) a NB domain; and (ii) a LRR domain, wherein the LRR domain includes a sub-domain that confers a heat-stable defense response to a plant pathogen; and (b) regenerating a plant from the transformed plant cell, wherein the plant exhibits resistance to the pathogen. In preferred embodiments, the expressed polypeptide confers disease resistance on a plant expressing said polypeptide at both 22° C. and 28° C. or at both 22° C. and 30° C. In yet other preferred embodiments, the polypeptide, when expressed in a plant, is localized in the plant cell nucleus.

In other preferred embodiments, the plant expressing the heat-stable NB-LRR polypeptide has an increased level of resistance compared to a corresponding control plant at the masking temperature of the control plant.

In still other embodiments, the nucleic acid molecule is introduced through breeding or through transformation or both. Preferably, the plant is a monocot or a dicot and the pathogen is a bacterial or a viral pathogen. Exemplary plants useful in the invention include, without limitation, crucifers such as Arabidopsis thaliana, Populus trichocarpa (black cottonwood), Solanum tuberosum (potatoes), Cucumis melo (Oriental melon), Medicago sativa (alfalfa), Populus balsamifera (balsam poplar), Phaseolus vulgaris (French bean), Glycine max (soybeans), Medicago truncatula, Nicotiana tabacum (tobacco), Nicotiana glutinosa, Solanum lycopersicum (tomato), Solanum tuberosum subsp. andigena (potato), Lens culinaris (lentil), Linum usitatissimum (flax), Vitis vinifera (wine grape), Oryza sativa Indica Group (Indian rice), or Oryza sativa Japonica Group (Japanese rice).

In another aspect, the invention features a substantially-pure polypeptide which includes: (a) a NB domain; and (b) a LRR domain, wherein the LRR domain includes a sub-domain that confers a heat-stable defense response to a plant pathogen. Preferably, the polypeptide confers disease resistance on a plant expressing said polypeptide at both 22° C. and 28° C. or at both 22° C. and 30° C. The polypeptide, when expressed in a plant, is also localized in the plant cell nucleus.

By a “substantially pure polypeptide” is meant a polypeptide such as a heat-stable NB-LRR disease resistance polypeptide (for example, a SNC1-3, SNC1 E640R, N Y638K, N N640D, or N Y738K N640D polypeptide or a polypeptide described in Appendix 4) that has been separated from components which naturally accompany it. Typically, the polypeptide is substantially pure when it is at least 60%, by weight, free from the proteins and naturally-occurring organic molecules with which it is naturally associated. Preferably, the preparation is at least 75%, more preferably at least 90%, and most preferably at least 99%, by weight, a heat-stable NB-LRR disease resistance polypeptide. A substantially pure heat-stable NB-LRR disease resistance polypeptide may be obtained, for example, by extraction from a natural source (for example, a plant cell); by expression of a recombinant nucleic acid encoding a heat-stable NB-LRR disease resistance polypeptide; or by chemically synthesizing the protein. Purity can be measured by any appropriate method, for example, column chromatography, polyacrylamide gel electrophoresis, or by HPLC analysis.

By “isolated nucleic acid molecule” is meant a nucleic acid molecule that is free of the genes which, in the naturally-occurring genome of the organism from which the nucleic acid molecule is derived from, flank the gene. The term therefore includes, for example, a recombinant DNA that is incorporated into a vector; into an autonomously replicating plasmid or virus; or into the genomic DNA of a prokaryote or eukaryote; or that exists as a separate molecule (for example, a cDNA or a genomic or cDNA fragment produced by PCR or restriction endonuclease digestion) independent of other sequences. It also includes a recombinant DNA which is part of a hybrid gene encoding additional polypeptide sequence.

By “derived from” is meant isolated from or having the sequence of a naturally-occurring sequence (for example, a cDNA, genomic DNA, synthetic DNA, or combination thereof).

By “masking temperature” is meant a temperature at which a defense response to a pathogen is ineffective to provide a plant with resistance to such pathogen.

By “polypeptide” or “protein” is meant any chain of amino acids, regardless of length or post-translational modification (for example, glycosylation or phosphorylation).

By “plant cell” is meant any self-propagating cell bounded by a semi-permeable membrane and containing a plastid. Such a cell also requires a cell wall if further propagation is desired. Plant cell, as used herein includes, without limitation, algae, cyanobacteria, seeds, suspension cultures, embryos, meristematic regions, callus tissue, leaves, roots, shoots, gametophytes, sporophytes, pollen, and microspores.

By “plant component” is meant a part, segment, or organ obtained from an intact plant or plant cell. Exemplary plant components include, without limitation, somatic embryos, leaves, stems, roots, flowers, tendrils, fruits, scions, and rootstocks.

By “crucifer” is meant any plant that is classified within the Cruciferae family. The Cruciferae include many agricultural crops, including, without limitation, rape (for example, Brassica campestris and Brassica napus), broccoli, cabbage, brussel sprouts, radish, kale, Chinese kale, kohlrabi, cauliflower, turnip, rutabaga, mustard, horseradish, and Arabidopsis.

By “transgene” is meant any piece of a nucleic acid molecule (e.g., DNA) which is inserted by artifice into a cell, and becomes part of the genome of the organism which develops from that cell. Such a transgene may include a gene which is partly or entirely heterologous (i.e., foreign) to the transgenic organism, or may represent a gene having sequence identity to an endogenous gene of the organism.

By “transgenic” is meant any cell which includes an isolated nucleic acid molecule (e.g., a DNA sequence) which is inserted by artifice into a cell and becomes part of the genome of the organism which develops from that cell. As used herein, the transgenic organisms are generally transgenic plants and the DNA (for example, a transgene) is inserted by artifice into the nuclear or plastidic genome. A transgenic plant according to the invention may contain one or more of the isolated nucleic acid molecules described herein.

By “pathogen” is meant an organism whose infection of viable plant tissue elicits a disease response in the plant tissue. Such pathogens include, without limitation, bacteria, mycoplasmas, fungi, oomycetes, insects, nematodes, viruses, and viroids. Examples of such plant diseases caused by these pathogens are described in Chapters 11-16 of Agrios, Plant Pathology, 3rd ed., Academic Press, Inc., New York, 1988.

Examples of bacterial pathogens include, without limitation, Erwinia (for example, E. carotovora), Pseudomonas (for example, P. syringae), and Xanthomonas (for example, X. campepestris and X. oryzae).

Examples of fungal or fungal-like disease-causing pathogens include, without limitation, Alternaria (for example, A. brassicola and A. solani), Ascochyta (for example, A. pisi), Botrytis (for example, B. cinerea), Cercospora (for example, C. kikuchii and C. zaea-maydis), Colletotrichum sp. (for example, C. lindemuthianum), Diplodia (for example, D. maydis), Erysiphe (for example, E. graminis f.sp. graminis and E. graminis f.sp. hordei), Fusarium (for example, F. nivale and F. oxysporum, F. graminearum, F. solani, F. monilforme, and F. roseum), Gaeumanomyces (for example, G. graminis f.sp. tritici), Helminthosporium (for example, H. turcicum, H. carbonum, and H. maydis), Macrophomina (for example, M. phaseolina and Maganaporthe grisea), Nectria (for example, N. heamatocacca), Peronospora (for example, P. manshurica, P. tabacina), Phoma (for example, P. betae), Phymatotrichum (for example, P. omnivorum), Phytophthora (for example, P. cinnamomi, P. cactorum, P. phaseoli, P. parasitica, P. citrophthora, P. megasperma f.sp. sojae, and P. infestans), Plasmopara (for example, P. viticola), Podosphaera (for example, P. leucotricha), Puccinia (for example, P. sorghi, P. striiformis, P. graminis f.sp. tritici, P. asparagi, P. recondita, and P. arachidis), Puthium (for example, P. aphanidermatum), Pyrenophora (for example, P. tritici-repentens), Pyricularia (for example, P. oryzea), Pythium (for example, P. ultimum), Rhizoctonia (for example, R. solani and R. cerealis), Scerotium (for example, S. rolfsii), Sclerotinia (for example, S. sclerotiorum), Septoria (for example, S. lycopersici, S. glycines, S. nodorum and S. tritici), Thielaviopsis (for example, T. basicola), Uncinula (for example, U. necator), Venturia (for example, V. inaequalis), and Verticillium (for example, V. dahliae and V. albo-atrum).

Examples of pathogenic nematodes include, without limitation, root-knot nematodes (for example, Meloidogyne sp. such as M. incognita, M. arenaria, M. chitwoodi, M. hapla, M. javanica, M. graminocola, M. microtyla, M. graminis, and M. naasi), cyst nematodes (for example, Heterodera sp. such as H. schachtii, H. glycines, H. sacchari, H. oryzae, H. avenae, H. cajani, H. elachista, H. goettingiana, H. graminis, H. mediterranea, H. mothi, H. sorghi, and H. zeae, or, for example, Globodera sp. such as G. rostochiensis and G. pallida), root-attacking nematodes (for example, Rotylenchulus reniformis, Tylenchuylus semipenetrans, Pratylenchus brachyurus, Radopholus citrophilus, Radopholus similis, Xiphinema americanum, Xiphinema rivesi, Paratrichodorus minor, Heterorhabditis heliothidis, and Bursaphelenchus xylophilus), and above-ground nematodes (for example, Anguina funesta, Anguina tritici, Ditylenchus dipsaci, Ditylenchus myceliphagus, and Aphenlenchoides besseyi).

Examples of viral pathogens include, without limitation, tobacco mosaic virus (TMV), tobacco necrosis virus (TNV), potato leaf roll virus, potato virus X, potato virus Y, tomato spotted wilt virus, and tomato ring spot virus.

As discussed herein, several genes encoding heat-stable NB-LRR disease resistance polypeptides has been identified, isolated or engineered, and characterized. Accordingly, the invention provides a number of important advances and advantages for the protection of plants against pathogens. For example, the invention facilitates an effective and economical means for in-plant protection against plant pathogens at temperatures at which heat masking or sensitivity to heat occurs. Such protection against pathogens reduces or minimizes the need for traditional chemical practices (for example, application of fungicides, bactericides, nematicides, insecticides, or viricides) that are typically used by farmers for controlling the spread of plant pathogens and providing protection against disease-causing pathogens. In addition, because plants which include heat-stable NB-LRR disease resistance polypeptides are less vulnerable to pathogens and their diseases, the invention further provides for increased production efficiency, as well as for improvements in quality and yield of crop plants and ornamentals. Thus, the invention contributes to the production of high quality and high yield agricultural products, for example, fruits, ornamentals, vegetables, cereals and field crops having reduced spots, blemishes, and blotches that are caused by pathogens; agricultural products with increased shelf-life and reduced handling costs; and high quality and yield crops for agricultural (for example, cereal and field crops), industrial (for example, oilseeds), and commercial (for example, fiber crops) purposes. Furthermore, because the invention reduces the necessity for chemical protection against plant pathogens, the invention benefits the environment where the crops are grown. Genetically-improved seeds and other plant products that are produced using plants expressing the genes described herein also render farming possible in areas previously unsuitable for agricultural production due to, for example, temperature extremes and global climate change.

Constructs

As is discussed above, the invention relates to vectors, especially plasmids, and other vectors common in genetic engineering, that contain the above-described isolated nucleic acid molecules encoding a heat-stable NB-LRR polypeptide. Preferably, such nucleic acid molecules contained in the vectors are operably linked to regulatory elements that provide for the transcription and expression of a polypeptide or protein in eukaryotic cells. Typically, the recombinant DNA molecule containing the isolated nucleic acid molecule will include in an operably linked manner, in the 5′ to 3′ direction of transcription, a transcription initiation control region capable of promoting, initiating and/or modulating transcription and translation in a plant cell (a promoter region), the nucleic acid molecule encoding a heat-stable NB-LRR polypeptide, and a transcription and translation termination region (otherwise referred to as a 3′ untranslated region). As used herein, a first nucleic acid sequence is “operably linked” with a second nucleic acid sequence when the sequences are so arranged that the first nucleic acid sequence affects the function of the second nucleic-acid sequence. Preferably, the two sequences are part of a single contiguous nucleic acid molecule and more preferably are adjacent. A “recombinant” nucleic acid or “recombinant DNA molecule” is made by an artificial combination of two otherwise separated segments of sequence, e.g., by chemical synthesis or by the manipulation of isolated segments of nucleic acids by genetic engineering techniques. The terms “recombinant DNA construct,” “recombinant vector,” “expression vector” or “expression cassette” refer to any agent such as a plasmid, cosmid, virus, BAC (bacterial artificial chromosome), autonomously replicating sequence, phage, or linear or circular single-stranded or double-stranded DNA or RNA nucleotide sequence, derived from any source, capable of genomic integration or autonomous replication, comprising a DNA molecule in which one or more DNA sequences have been linked in a functionally operative manner.

As used herein, a “promoter” refers to a DNA sequence that binds an RNA polymerase (and often other transcription factors as well) and promotes transcription of a downstream DNA sequence. The resulting transcribed sequence can be an RNA that has function, such as rRNA (ribosomal RNA) or tRNA (transfer RNA). Often, the RNA produced is a heteronuclear (hn) RNA that has introns that are spliced out to produce an mRNA (messenger RNA). A “plant promoter” is a native or non-native promoter that is functional in plant cells. Constitutive promoters are functional in most or all tissues of a plant throughout plant development. Tissue-, organ- or cell-specific promoters are expressed only or predominantly in a particular tissue, organ, or cell type, respectively. Specific expression is used herein to refer to any promoter that provides an increased expression in a single tissue or developmental stage, or under a particular environmental condition, but causes expression, even significant expression, in other tissue(s), or developmental stage(s), or environmental condition(s).

Temporally regulated promoters are functional only or predominantly during certain periods of plant development or at certain times of day. Inducible promoters selectively express an operably linked DNA sequence in response to the presence of an endogenous or exogenous stimulus, for example, by chemical compounds (chemical inducers) or in response to environmental, hormonal, chemical, and/or developmental signals. Inducible or regulated promoters include, for example, promoters regulated by light, heat, stress, flooding or drought, phytohormones, wounding, cold, or chemicals such as ethanol, jasmonate, salicylic acid, or safeners.

For the most part, any plant promoter can be used as a 5′ regulatory sequence to modulate expression of a particular gene or genes, such as a plant RNA polymerase II promoter. When fused to heterologous DNA sequences, such promoters typically cause the fused sequence to be transcribed in a manner that is similar to that of the gene sequence with which the promoter is normally associated. Promoter fragments that include regulatory sequences can be added (for example, fused to the 5′ end of, or inserted within, an active promoter having its own partial or complete regulatory sequences). Alternatively, heterologous regulatory sequences can be added to the 5′ upstream region of an inactive, truncated promoter, e.g., a promoter including only the core TATA and, sometimes, the CCAAT sequences.

Promoters are typically comprised of multiple distinct cis-acting transcriptional regulatory elements, which can confer a different aspect of the overall control of gene expression. The promoter sequences of the present invention may contain cis elements that modulate gene expression. Cis elements can be part of the promoter, or can be upstream or downstream of said promoter. Cis elements (or groups thereof), acting at a distance from a promoter are often referred to as repressors or enhancers. Enhancers act to upregulate the transcriptional initiation rate of RNA polymerase at a promoter, while repressors act to decrease said rate. In some cases, the same elements can be found in a promoter and an enhancer or repressor. Cis elements are generally sites where transcription factors bind to the DNA and modulate the rate at which RNA polymerase binds to the promoter.

Examples of constitutive promoters that are active in plant cells include but are not limited to the nopaline synthase (NOS) promoters; the cauliflower mosaic virus (CaMV) 19S and 35S (sometimes called 35S herein); the tobacco mosaic virus promoter; the figwort mosaic virus promoters; and actin promoters, such as the Arabidopsis actin gene promoter.

The term “tissue-specific promoter” means a regulatory sequence that causes an enhancement of transcription from a downstream gene in specific cells or tissues at specific times during plant development, such as in vegetative tissues or reproductive tissues. Examples of tissue-specific promoters under developmental control include promoters that initiate transcription only (or primarily only) in certain tissues, such as vegetative tissues, e.g., roots, leaves or stems, or reproductive tissues, such as fruit, ovules, seeds, pollen, pistols, flowers, or any embryonic tissue. Reproductive tissue specific promoters may be, e.g., ovule-specific, embryo-specific, endosperm-specific, integument-specific, seed coat-specific, pollen-specific, petal-specific, sepal-specific, style-specific, or some combination thereof. One skilled in the art will recognize that a tissue-specific promoter may drive expression of operably linked sequences in tissues other than the target tissue. Thus, as used herein a tissue-specific promoter is one that drives expression preferentially in the target tissue, but may also lead to expression in other tissues as well.

In a preferred embodiment of the invention, the nucleic acid molecule encoding a heat-stable NB-LRR polypeptide is operably linked to a tissue-specific promoter, or promoter that directs expression in the leaf tissue or a region therein.

Other examples of possible suitable regulatory sequences include introns, 3′ non-coding regions such as poly A sequences, insulator regions and the like. Molecular biological techniques for identifying, obtaining and using such regulatory elements in combination with the nucleic acid molecules of the present invention are known in the art.

Transformation Methods and Transgenic Plants

The present invention further relates to transgenic plant cells and transgenic plants having been transformed to contain and express a heat-stable NB-LRR polypeptide. “Transformed,” “transfected,” or “transgenic” refers to a cell, tissue, organ, or organism into which has been introduced a foreign nucleic acid, such as a recombinant vector. A transgenic plant according to the invention may contain one or more of the nucleic acid molecules described herein. Preferably, the introduced nucleic acid is integrated into the genomic DNA of the recipient cell, tissue, organ or organism such that the introduced nucleic acid is inherited by subsequent progeny. A “transgenic” or “transformed” cell or organism also includes progeny of the cell or organism and progeny produced from a breeding program employing such a “transgenic” plant as a parent in a cross and exhibiting an altered phenotype resulting from the presence of a recombinant construct or vector. The method of transformation is not critical to the current invention and various methods of plant transformation are currently known and available. For example, the introduction of DNA sequences into plants and/or plant cells can be accomplished by Agrobacterium mediated transformation, viral vector mediated transformation, electroporation, and microprojectile bombardment mediated transformation (particle gun or biolistics methods). The DNA sequence may also be transformed directly into the plastid genome by plastid transformation.

Whole plants can be regenerated, for example, from single cells, callus tissue, or leaf discs transformed with a plant expression vector according to standard plant tissue culture techniques. It is well known in the art that various cells, tissues, and organs from almost any plant can be successfully cultured to regenerate an entire plant; according to standard techniques.

This invention is applicable to dicotyledonous and monocotyledonous species and is readily applicable to new and/or improved transformation techniques. For efficient production of transgenic plants from plant cells or plant tissue, it is desirable that the plant tissue used for transformation possess a high capacity for regeneration. Techniques are known in the art to regenerate plants from transformed plant tissue cultures of plant cells.

The transgenic plants produced in accordance with this invention may, as previously stated, be any dicotyledonous or monocotyledonous species and are preferably from useful species such as maize (corn), peas, soybean, alfalfa, cassava, potato, cotton, and cereals (e.g., barley, oats, rye, triticale and wheat). Corn refers to Zea Mays and all species and varieties that can be bred with it. Wheat refers to all of Triticum aestivum varieties including but not limited to spring, winter, and all facultative wheat varieties. Wheat includes any other wheat species, including but not limited to durum wheat (Triticum durum), spelt (Triticum spelta), emmer (Triticum dicoccum), and wild wheat (Triticum monococcum). Wheat also includes any species that can be bred with any of the aforementioned wheat species. Soybeans refers to Glycine max and any species or variety that can be bred with it. Rice refers to Oryza sativa and any species or variety that can be bred with it. Barley refers to Hordeum vulgare and any species or variety that can be bred with it. Oats refers to Avena sativa and any species or variety that can be bred with it. Canola is a coined name recently given to seed, oil, and meal produced by genetically modified rapeseed plants, oilseed rape (Brassica napus L.) and turnip rape (B. campestris L), herein canola includes all rapeseed plants and organisms that can be bred with them. Agrobacterium tumefaciens as used herein includes all strains and types of this species. Cotton refers to all plants in the genus Gossypium and all plants that can be bred with them.

A method according to the invention comprises introducing a DNA molecule containing a promoter functional in plant cells operably linked to a nucleic acid sequence encoding a heat-stable NB-LRR polypeptide (exemplary isolated DNA molecules are described in Appendix 4), and producing a plant (as well as fertile progeny plant of such a plant) from the transformed plant cell. Progeny includes fertile descendants of a particular plant or plant line.

The invention further relates to the production of transgenic seed. “Transgenic seed” means a plant seed whose nucleus has been altered by the incorporation substantially pure nucleic acid molecule encoding a polypeptide comprising a NB-LRR domain which includes a heat-stable subdomain of the LRR, the polypeptide modulating a defense response in a plant expressing such polypeptide, e.g., by transformation as described herein. The term “transgenic plant” is used to refer to the plant produced from an original transformation event, or progeny from later generations or crosses of a plant to a transformed plant, so long as the progeny contains a nucleus with the recombinant DNA in its genome.

The invention further relates to a transgenic plant component. By “plant component” is meant a part, segment, or organ obtained from an intact plant or plant cell. Exemplary plant components include, without limitation, somatic embryos, leaves, stems, roots, flowers, tendrils, fruits, scions, tubers, and rootstocks.

Other features and advantages of the invention will be apparent from the following Drawings, Detailed Description, and the Claims.

BRIEF DESCRIPTION OF THE DRAWINGS

FIGS. 1A-1E show that the int102 mutant has a temperature-insensitive defense response.

FIG. 1A shows the dwarf phenotype of snc1-1 at 22° C. is suppressed by a higher temperature of 28° C. Shown are 4-week-old plants.

FIG. 1B shows the int102 mutation enables snc1-1 to retain resistance to a virulent pathogen at 28° C. Shown is the growth of Pseudomonas syringae pv tomato (Pst) DC3000 in the wild type, snc1-1, and int102-1 snc1-1 at 22° C. and 28° C.

FIG. 1C shows the int102 mutation confers a dwarf phenotype to snc1-1 at 28° C. Shown are 3-week-old plants.

FIG. 1D shows that the expression of defense genes is upregulated in int102-1 snc1-1 at both 22° C. and 28° C. and this upregulation in int102-1 snc1-1 is dependent on PAD4. Expression of PR1 and SNC1 is analyzed by RNA blot.

FIG. 1E shows the dwarf phenotype of int102-1 snc1-1 at 28° C. is suppressed by pad4 and nahG. Shown are wild type, int102-1 snc1-1pad4, and int102-1 snc1-1 nahG grown at 28° C. after bolting.

FIGS. 2A-2C show that the snc1-3 mutation confers temperature-insensitive activity to SNC1.

FIG. 2A shows that the hypersensitive response (HR) is induced by SNC1 with the snc1-3 mutation at 28° C. Four p35S::SNC1:GFP constructs: SNC1 wild-type (WT), SNC1-1, SNC1-3 and SNC1-4 (containing both snc1-1 and snc1-3 mutations), were infiltrated via Agrobaterium (agro-infiltrated) into Nicotiana benthamiana (Nb) leaves. Shown are leaves at 3 days after infiltration. HR is indicated by arrows.

FIG. 2B shows the subcellular localization of the SNC1:GFP proteins in Nb at 22° C. and 28° C. Infiltrated leaves as described in FIG. 2A were analyzed by fluorescent microscopy one day before the onset of HR. SNC1-3 and SNC1-4 but not SNC1-1 were retained in the nucleus at 28° C. SNC1WT had a weaker signal and a longer exposure time was used to take the image.

FIG. 2C shows the subcellular localization of the SNC1:GFP proteins in Arabidopsis thaliana protoplasts. The same set of four constructs as in FIG. 2A were transformed into Arabidopsis protoplasts and the GFP signals were observed at 12 hours after transformation by fluorescent microscopy. SNC1WT was exposed for a longer time than the other three samples.

FIG. 2D shows a nucleus export signal (NES) abolishes the activities of SNC1-3 and SNC1-4. SNC1-3:GFP, SNC1-3:GFP:NES, SNC1-4:GFP, and SNC1-4:GFP:NES were agro-infiltrated in Nb and their HR inducing activities were assayed at 22° C. and 28° C. The left half of each leaf was infiltrated with the SNC1:GFP fusion, and the right half of the leaf was infiltrated with the corresponding SNC1:GFP fusion with NES. Shown are leaves at 3 days after infiltration. HR indicated by arrows was only observed with fusion proteins without NES. Abbreviations: WT, SNC1WT:GFP; -1, SNC1-1:GFP; -3, SNC1-3:GFP; -4, SNC1-4:GFP; -3:NES, SNC1-3:GFP:NES; -4:NES, SNC1-4:GFP:NES.

FIG. 3A-3C show that the MOSS and MOS6 genes are required for the SNC1-3 protein activity.

FIG. 3A shows that the dwarf phenotype of snc1-4 is suppressed by mos3 or mos6. Shown are 3-week-old seedlings of the wild type, snc1-4 mos3, snc1-4 mos6, and snc1-4 at 22° C. and 28° C.

FIGS. 3B and 3C show the subcellular localization of the SNC1-1:GFP protein at 22° C. (FIG. 3A) and SNC1-3:GFP at 28° C. (FIG. 3C) in wild-type (wt), mos3, mos6, and pad4 plants. SNC1WT:GFP, SNC1-1:GFP, and SNC1-3:GFP were expressed at 22° C. or 28° C. in protoplasts isolated from the mos3, mos6, and pad4 mutant plants and the GFP signals were observed at 12 hours after transformation by fluorescent microscopy. The SNC1-1 and SNC1-3 proteins were present in the nucleus in the pad4 mutant as in the wild type, but were mostly in the cytosol and plasma membrane in mos3 and mos6. Abbreviations: wt, wild type; others are the same as in FIG. 2.

FIGS. 4A-4B show that the mutations in the N gene confer temperature-insensitive defense responses.

FIG. 4A shows HR induced by the WT and three mutant N genes at 22° C. and 30° C. in Nt. The WT and mutant N genes were agro-infiltrated in Nt together with its elicitor p50. The WT N gene induced HR at 22° C. but not 30° C., while the Y638K, N640D, and Y638KN640D mutants induced HR at both temperatures.

FIG. 4B shows the localization of N-citrine in Nb at 22° C. and 30° C. when co-expressed with p50. The N-citrine chimeric gene was agro-infiltrated in Nb with p50, and the citrine signal was monitored up to three days. The nuclear localization of the N-citrine protein was observed at 22° C. but not at 30° C.

FIG. 5 shows that the nucleus export signal (NES) suppresses the nuclear localization of the SNC1-3 and SNC1-4 proteins. Shown are the localization of SNC1-3:GFP, SNC1-4:GFP, SNC1-3:GFP:NES, and SNC1-4:GFP:NES proteins expressed in Nb at 28° C. While SNC1-3:GFP and SNC1-4:GFP were mostly localized to the nucleus, SNC1-3:GFP:NES and SNC1-4:GFP:NES had reduced expression in the nucleus and are also found in the cytosol and the plasma membrane. Abbreviations are the same as in FIG. 2.

FIG. 6 shows that the MOS3 and MOS6 genes are required for the SNC1-3 and SNC1-4 activities. Subcellular localization of SNC1-3:GFP at 22° C. (A) and SNC1-4:GFP proteins at 22° C. (B) and 28° C. (C) in wild type (wt), mos3, mos6, and pad4. SNC1-3:GFP, and SNC1-4:GFP were expressed at 22° C. and 28° C. in protoplasts isolated from the mos3, mos6, and pad4 mutant plants, and the GFP signals were observed at 12 hours after transformation by fluorescent microscopy. The SNC1-3 and SNC1-4 proteins were present in the nucleus in the pad4 mutant as in the wild type, but were mostly in the cytosol and plasma membrane in mos3 and mos6 at both temperatures. Abbreviations: wt, wild type; others are the same as in FIG. 2.

DETAILED DESCRIPTION Overview

The plant immune system consists of multiple layers of responses to various biotic attacks, enabling a success in plant survival, fitness and reproduction (1, 2). These defense responses are modulated by abiotic environmental factors such as light, humidity, and temperature (3-7). As is mentioned above, a high temperature suppresses a number of plant defense responses rendering a normally resistant plant susceptible to pathogen attacks. This temperature sensitivity poses a challenge to agriculture and yet the molecular mechanisms underlying this temperature modulation are unknown. Below it is demonstrated that the disease resistance (R) gene known to recognize pathogen effectors (8, 9) is a temperature sensor conferring temperature sensitivity in disease resistance. A loss of nuclear localization of an Arabidopsis R protein named SNC1 (10) and a tobacco R protein named N (11) at a high growth temperature is responsible for the suppression of defense responses mediated by these R proteins at high temperatures. Further, specific residue alterations in the SNC1 and the N proteins counteract this temperature effect and sustain defense responses at high temperatures. These findings are useful to generate effective plant immune responses within a broader temperature range.

As is discussed in greater detail below, an Arabidopsis thaliana mutant snc1-1 was used as a starting strain to isolate mutants that retain enhanced disease resistance at higher temperatures. snc1-1 has a missense mutation in the NB-LRR type of R protein SNC1, as well as a constitutive defense response and a dwarf phenotype at normal growth temperature 22° C. but is disease susceptible with a normal growth phenotype at a higher temperature such as 28° C. This mutant screen yielded mutants with a snc1-1 dependent growth and defense mutant phenotype at both 22° C. and 28° C. One mutant identified from this screen was cloned as a new allele (snc1-4) of SNC1 with an E640 mutated to K (referred as the snc1-3 mutation) in the SNC1 protein (Table 1). This snc1-3 mutation alone is sufficient to induce enhanced disease resistance at both low and high temperatures without the original snc1-1 mutation. This finding revealed for the first time that an alteration in the R protein rather than other players in plant innate immunity is sufficient to confer temperature insensitivity. Thus, the R gene is a temperature sensor in defense responses. In addition, specific mutations in the R proteins SNC1 alter temperature sensitivity, making them active at both low and high temperatures.

The molecular basis for this temperature sensitivity in SNC1 was also examined. Temperature was found to influence the subcellular localization of the SNC1 protein: the nuclear localization of SNC1 correlated with its biological activity. The SNC1-1 protein that is active only at 22° C. is concentrated in the nucleus at 22° C. but is out of the nucleus at 28° C. while the SNC1-3 protein that is active at both 22° C. and 28° C. stays in the nucleus at both temperatures. The addition of a nucleus export signal to the SNC1-3 protein resulted in exclusion of the SNC1-3 protein from the nucleus, leading to a loss of SNC1 activity at 28° C. Thus, temperature modulation of R protein localization is the basis for temperature sensitivity of R proteins and consequently temperature sensitivity of disease resistance.

These findings in the Arabidopsis SNC1 have a general application for disease resistance mediated by other NB-LRR R proteins. For example, the tobacco N gene (11) mediates resistance to cauliflower mosaic virus, and this resistance is suppressed by a higher temperature of 30° C. Cognate mutations of snc1-3 when introduced into the N gene enable a heat-stable resistance (Table 1), indicating a universal mechanism in temperature sensitivity of disease resistance. Although the molecular consequences induced by these mutations are not well understood, it is believed that a change of the charges from negative to positive around the E640 residue in the LRR region alters the conformation of the R protein or its interaction with other proteins. By mutating E640 to R in SNC1 a heat-stable HR (Table 1) was obtained, supporting this hypothesis.

The details of the aforementioned experiments now follow.

Experimental

A genetic screen in snc1-1 (10) for mutants defective in high temperature suppression of defense responses was carried out. The wild-type Arabidopsis plants do not have constitutive defense responses as these responses usually compromise plant growth and sometimes cause cell death. The Arabidopsis snc1-1 mutant has a constitutive defense response and a dwarf phenotype under normal growth temperature 22° C. due to a missense mutation in the linker region of SNC1 (10), and both phenotypes are suppressed by a higher growth temperature such as 28° C. (7) (FIG. 1A, B). One such mutant isolated, int (insensitive to temperature)102-1, has a snc1-1 dependent dwarf phenotype at both 22° C. and 28° C. (FIG. 1C). The int102-1snc1-1 mutant is as resistant to Pseudomonas Syringae pv. tomato (Pst) DC3000 as snc1-1 at 22° C., but retains resistance at 28° C. in contrast to snc1-1 (FIG. 1B). Therefore, the int102-1snc1-1 mutant indeed has a temperature-insensitive (heat-stable) constitutive defense response. Consistently, the expressions of PR1 and SNC1, two genes responsive to an increase of salicylic acid (SA) associated with enhanced disease resistance (7, 12), were higher in int102-1snc1-1 than in the wild type or snc1-1 at 28° C. (FIG. 1D). Both the defense and the growth phenotypes of int102-1snc1-1 can be suppressed by nahG (13) coding a SA degradation enzyme and by pad4 (14) defective in defense responses (FIG. 1D, E, and data not shown), further demonstrating an upregulation of defense responses in the int102-1snc1-1 mutant at 28° C.

We cloned the INT102 gene based on its tight linkage to SNC1 in a mapping population (online methods). Sequencing the SNC1 gene in int102-1snc1-1 revealed a G to A point mutation causing a change of glutamic acid to lysine (named as snc1-3) at amino acid residue 640 in the LRR domain of SNC1 (Table 1).

TABLE 1 Mutations isolated or generated in the  SNC1 and the N proteins. starting HR at high Genes residue # Sequences temperatures SNC1 WT 639 EELD no SNC1-3 EKLD yes SNC1 E640R ERLD yes N WT 637 EYVN no N Y638K EKVN yes, weak N N640D EYVD yes N Y738K EKVD yes N640D Shown are the aligned regions of SNC1 and N proteins with mutated residues underlines. The wild-type and the mutant genes were tested for HR-inducing activities at 28° C. (for SNC1) and 30° C. (for N).

The int102-1snc1-1 mutant is therefore named snc1-4, and it contains both the snc1-1 and snc1-3 mutations. To confirm that the snc1-3 mutation is responsible for the temperature-insensitive disease resistance phenotype, we generated transgenic plants carrying the genomic fragments of either the wild-type or the mutant SNC1-4 genes in the wild-type Col-0 plants. However, transgenic plants carrying the wild-type SNC1 gene exhibited a dwarf phenotype similar to those carrying the SNC1-4 mutant gene (data not shown), and this auto-activation of the SNC1 as a transgene is likely due to a loss of transcriptional repression imposed at its endogenous chromosomal location (15). We subsequently developed a transient assay for the SNC1 gene activity in Nicotiana benthamiana (Nb) by the hypersensitive response (HR), a form of programmed cell death induced by the activation of R proteins. The SNC1 protein was tagged by the green fluorescent protein (GFP) at the carboxyl-terminus and expressed under the strong CaMV 35S promoter. This p35S::SNC1:GFP fusion gene was expressed in Nb leaves by Agrobacterium-mediated infiltration (agro-infiltration), and HR symptoms such as collapsed leaves was monitored at 22° C. and 28° C. respectively over a period of 3 days after infiltration. In contrast to the wild-type SNC1 (SNC1WT) gene that did not cause any HR, the SNC1-1 mutant gene induced HR at 22° C. but not at 28° C. while the SNC1-3 and SNC1-4 genes each induced HR at both temperatures (FIG. 2A). Thus, snc1-3 is indeed the mutation responsible for the int102-1snc1-1 phenotype. Furthermore, the snc1-3 mutation alone (without snc1-1) is sufficient to induce temperature-insensitive defense responses. This result indicates that temperature sensitivity of disease resistance is controlled by the R gene rather than other regulatory components and that a mutation in an NB-LRR type of R gene is sufficient to confer temperature-insensitive disease resistance.

We further investigated the molecular basis underlying the temperature sensitivity of the NB-LRR type of R gene SNC1. A correlation was observed between the nuclear localization of the SNC1 protein and its HR-inducing activity in Nb at both temperatures. A very weak GFP signal was detected in the cytosol and the plasma membrane for the SNC1WT:GFP fusion protein (FIG. 2B). The SNC1-1:GFP mutant fusion protein was localized to the nucleus at 22° C. (FIG. 2B), confirmed by nucleus staining with 4′,6-diamidino-2-phenylindole (DAPI) (data not shown), but it was found in the cytosol and the plasma membrane at 28° C. (FIG. 2B). In contrast, both SNC1-3:GFP and SNC1-4:GFP were localized to the nucleus at both 22° C. and 28° C. (FIG. 2B). The localization of these SNC1 proteins was confirmed in a transient expression system in Arabidopsis thaliana. When expressed at 22° C. in Arabidopsis protoplasts, SNC1-1:GFP, SNC1-3:GFP, and SNC1-4:GFP, but not SNC1WT:GFP, were localized predominantly in the nucleus (FIG. 2C). At 28° C., only SNC1-3:GFP and SNC1-4:GFP, but not SNC1WT:GFP or SNC1-1:GFP, were found in the nucleus (FIG. 3B, 3C, FIG. 6). It appears that temperature influences the localization of the SNC1 protein and the snc1-3 mutation causes a nuclear localization of SNC1 even at a higher temperature.

To determine whether the nuclear localization of SNC1 is the cause or the consequence of the enhanced defense responses at elevated temperatures, we added a nucleus export signal (NES) (16) to the SNC1:GFP fusions and expressed these constructs in Nb leaves. The addition of NES largely reduced the nuclear localization of SNC1-3:GFP and SNC1-4:GFP at 28° C., resulting in their expression in cytosol and plasma membrane as well (FIG. 5). Neither SNC1-3:GFP:NES nor SNC1-4:GFP:NES induced HR in Nb leaves, in contrast to SNC1-3:GFP and SNC1-4:GFP (FIG. 2D). Thus, nuclear localization is critical for the mutant SNC1 proteins to induce defense responses at a higher temperature. This finding is consistent with the emerging finding that nuclear localization of some R proteins is essential for them to confer disease resistance (17, 18).

Nuclear-cytosyl partition of proteins has critical roles for diverse plant developmental signaling and environmental responses, and a few genes involved in the nuclear-cytosyl shuttling processes are shown to be required for defense responses (19, 20). For instance, mutations in MOS3 (encoding a putative nucleoporin Nup96) or MOS6 (encoding a putative importin α3) could suppress enhanced disease resistance in snc1-1 (21, 22), although the exact mechanisms are not well understood. We tested whether genes involved in nuclear-cytosol transport are essential for defense responses induced by the SNC1 mutant protein at high temperatures. The mos3 and mos6 mutations were each introduced into the snc1-4 mutant, and both the snc1-4 mos3 and the snc1-4 mos6 double mutants exhibited a wild-type growth phenotype at 22° C. and 28° C. (FIG. 3A), indicating a requirement of functional MOS3 and MOS6 for the SNC1-4 activities at both temperatures. To determine whether MOS3 and MOS6 regulate SNC1-mediated defense response through SNC1 localization, we expressed different forms of p35S::SNC1:GFP in protoplasts isolated from the wild-type, mos3, and mos6 plants. The nuclear localization of SNC1-1 at 22° C. in the wild type was largely suppressed by the mos3 and mos6 mutations (FIG. 3B), indicating that MOS3 and MOS6 likely regulate snc1-1 mediated defense through the localization of the SNC1-1 protein. Similarly, nuclear localization of the SNC1-3 and SNC1-4 proteins at 22° C. and 28° C. in the wild type were greatly reduced in the mos3 and mos6 mutants, and the SNC1-3 and SNC1-4 proteins had enhanced cytosol and plasma membrane localization in the two mutants (FIG. 3C, and FIG. 6). Thus, the activities of SNC1-3 and SNC1-4 at a high temperature requires the two genes involved in nuclear-cytosyl transport. In contrast to the mos3 and mos6 mutations, the loss-of-function mutation of PAD4 that functions downstream of R protein activation did not alter the nuclear localization of the SNC1 mutant proteins although it suppresses the snc1 mutant phenotype similarly to mos3 and mos6 (FIG. 1E, 3B, 3C, and FIG. 6). These data indicate that MOS3 and MOS6 mediate SNC1-induced defense responses via regulating the R protein SNC1. It further demonstrates that nuclear localization of the SNC1 protein at high temperature is the cause rather than the consequence of heat-stable defense responses.

To determine whether the finding on temperature sensitivity in defense responses induced by the Arabidopsis SNC1 is a general phenomenon for disease resistance, we introduced similar mutations of snc1-3 to a tobacco R gene N that confers resistance to tobacco mosaic virus (TMV). It is well known but not understood how the N-containing plants lose resistance at a higher temperature of 30° C. (11). We altered two residues in the N protein by site-directed mutagenesis: one is the Y638K mutation corresponding to the snc1-3 mutation (E640K) of SNC1 and the other is the N640D mutation corresponding to D642 of SNC1 (Table 1). When co-expressed with its elicitor p50 in Nicotiana tabacum (Nb) by agro-infiltration, the wild-type N gene triggered HR at 22° C. but not at 30° C. (FIG. 4A, Table 1). In contrast, the three mutant N genes with Y638K, N640D, or Y638K N640D mutations induced HR in Nb at both 22° C. and 30° C. together with the N elicitor p50 (FIG. 4A, Table 1). These mutations do not appear to confer constitutive auto-activities because they did not cause HR in the absence of p50 (data not shown). Thus, the N gene is responsible for the temperature sensitivity of TMV resistance, indicating that other NB-LRR type of R genes function as temperature sensors in disease resistance and that temperature sensitivity can be altered by specific mutations in the R proteins to make heat-stable disease resistance.

We determined whether temperature sensitivity of the N gene is correlated with the N protein localization similar to that of the SNC1 gene. When expressed together with p50 in N. benthamiana, the N-citrine fusion protein was localized to the nucleus at 22° C. (FIG. 4B), consistent with previous findings (18). However, no signal could be detected in the nucleus when plants were incubated at 30° C. (FIG. 4B). This indicates that nuclear localization of activated wild-type R protein(s) is subject to temperature modulation, similarly to that of the active form of the mutant R protein such as SNC1-1.

The molecular basis of temperature-insensitive mutants of R proteins is not totally understood. This is not merely due to an over-activation of R proteins because the SNC1-1 mutant protein apparently has the same activity as SNC1-4 at 22° C. and yet has no activity at 28° C. The E640K mutation in SNC1 can potentially induce local post-translational protein modification such as ubiquitination, sumoylation, acetylation, and biotylation. Especially the ‘EKID’ sequence around snc1-3 and intriguingly the ‘LKIG’ sequences around snc1-1 are predicted to be sumoylation sites (http://www.abgent.com/tools/sumoplot_login). However, the N640D alone in N without the Y638K mutation is sufficient to induce HR at high temperatures, indicating that sumoylation is not the basis or the only basis for the activity. We therefore tested whether a charge change rather than a local protein modification is responsible for temperature insensitivity by introducing an E640R mutation to SNC1 (Table 1). Similar to SNC1-3:GFP, SNC1E640R:GFP induced HR at 28° C. and was localized to the nucleus when expressed in Nb (data not shown). Both E to K and E to R mutations add positive charges to the region and could potentially generate a local nuclear localization signal (23)²³. To test whether these mutations generate such a signal or are sufficient to induce nuclear localization, we created shorter versions of the SNC1:GFP proteins consisting of the linker region and the LRR domain of the SNC1 protein. Neither the snc1-3 nor the snc1-1 mutations conferred a nuclear localization to the shorter SNC1:GFP fusion proteins (data not shown), indicating that these mutations do not function autonomously to induce SNC1 nuclear localization.

The R protein activation involves alteration of intra-molecular interactions, with opening of the NB domain and possibly allowing interaction of the amino-terminal domain with downstream signaling molecules (24, 25). It is possible that a high temperature can influence the intra-molecular interactions and keep the R protein in an inactive closed form. A protein 3-D structure modeling suggested that the SNC1 E640 and a few nearby residues including D642 could form a more negatively charged pocket and this pocket might have a direct contact with positively charged residue(s) in the ARC domain. The E640K/R mutations could disrupt the interaction between the LRR domain and the ARC domain, leading to an active conformation of the SNC1 protein at a high temperature. Alternatively, these mutations could alter the interaction of SNC1 with downstream signaling molecules, leading to an active signaling event at high temperatures.

Future studies should further reveal the molecular basis of temperature sensitivity of R proteins and defense responses as well as temperature modulation of protein activities in general. The knowledge gained will potentially provide us with tools to engineer crop plants with temperature-insensitive disease resistance and with better adaptation to climate changes.

The above-described experimental results were obtained using the following materials and according to the following methods.

Material and Methods

The Arabidopsis thaliana plants were grown on soil at 22° C. or 28° C. under constant light for morphological phenotypic analysis, and under a photoperiod of 12 hour (hr) light/12 hr dark for disease resistance test. Arabidopsis seedlings used for protoplast transformation were grown on solid medium under a photoperiod of 8 hr light/16 hr dark. The Nicotiana tabacum (Nt) and Nicotiana bethamiana (Nb) plants were grown in the greenhouse. For chemical mutagenesis, the snc1-1 seeds were treated with 0.25% EMS (ethane methyl sulfonate) for 12 hours. For cloning the INT102 gene, the int102-1snc1-1 mutant in Col-0 was crossed to the Ws-2 wild type and standard mapping method (26) was used to identify the intervals containing the INT102 gene. The p35S::SNC1:GFP construct consists of the strong 35S CaMV promoter, the genomic fragment of the SNC1 coding region (from the translation start site to the last amino acid), and the green fluorescent protein (GFP) fused in frame to the carboxyl-terminus of SNC1. Site-directed mutagenesis was carried out with ‘QuikChange’ kit according to manufacture's instruction (Stratagene). The Arabidopsis protoplasts were generated from plate-grown seedlings according to methods by Zhai and Vatamaniuk (in press). RNA blot analysis, pathogen resistance test, and transient expression in Nb and Nt was performed as described (7, 27, 28).

Plant material and growth condition. The Arabidopsis thaliana plants were grown on soil at 22° C. or 28° C. under constant light with a relative humidity between 40% and 60% for morphological phenotypic and gene expression analysis. Arabidopsis seedlings used for protoplast transformation were grown on solid medium with ½ MS salts, 2% sucrose, and 0.8% agar and under a photoperiod of 8 hr light/16 hr dark. Nicotiana tabacum (Nt) and Nicotiana bethamiana (Nb) plants were grown in the greenhouse.

Mutant screen. The snc1-1 seeds were treated with 0.25% EMS (ethane methyl sulfonate) for 12 hours. Approximately 40,000 M2 plants (derived from 4,000 MO were screened at 28° C. for the snc1-1 like dwarf phenotype. Putative mutants were then crossed to the wild-type Col-0, and the F₂ population was analyzed to determine whether they are snc1-1 dependent or not.

Map-based cloning. The mapping population was created by crossing the int102-1 mutant in the Col-0 accession to the wild type of the Ws-2 accession. Dwarf plants among the F₂ progenies grown at 28° C. were chosen for mapping. Bulked segregation analysis was preformed on pools of 40 plants with SSLP, CAPS, and dCAPS markers between Col-0 and Ws-2 (26). The INT102 gene was found to be linked to marker VRN2 that is 1 cM from the SNC1 gene. Further analysis of 240 dwarf plants revealed no recombination between INT102 and SNC1, indicating a tight linkage of the two genes.

Generation of constructs. A 5.5 kb fragment containing the SNC1 coding region and the 3′UTR was isolated from the BAC clone F5D3 from ABRC. A BamHI restriction site was added to this genomic fragment before the stop codon of SNC1 via polymerase chain reaction (PCR). The NcoI-BamHI fragment containing the SNC1 coding region without the stop codon was inserted into pSAT-N1 vector (29) to generate the p35S::SNC1:GFP construct. The SNC1-1, SNC1-3, and SNC1-4 mutations were introduced into p35S::SNC1:GFP through site-directed mutagenesis with the ‘QuikChange’ kit according to manufacture's instruction (Stratagene). The cassettes of various p35S::SNC1:GFP were excised at the PI-PspI sites and cloned into the pHPT binary vector (29) to generate pHPT-SNC1, pHPT-SNC1-1, pHPT-SNC1-3, and pHPT-SNC1-4 constructs.

Transient expression in Nb and Nt. Each of these above binary vectors was then transformed into Agrobacterium tumefaciens stain C58C1 (30). Cultures of the transformed A. tumefaciens were grown overnight to OD₆₀₀ of 1.0 in liquid LB. Cells were then collected by centrifugation and resuspended in the induction medium (10 mM MES, pH5.7, 10 mM MgCl₂, 200 μM acetosyringone) to OD₆₀₀ of 0.5. After sitting at room temperature for 3 hrs, the Agrobacterial cells were infiltrated into the abaxial surface of Nb or Nt leaves using 1 ml needleless syringes. Infiltrated plants were subsequently incubated at 22° C. or 28° C. before infiltrated leaves were examined for GFP signals under a microscope (model BX61, Olympus) within a 48 hr period after inoculation.

RNA analysis. Total RNAs were extracted using Tri Reagent (Molecular Research, Cincinnati, Ohio) from leaves of 3-week-old plants. Twenty micrograms of total RNAs per sample were used for RNA gel blot analysis.

Pathogen resistance assay. P. syringae pv. tomato DC3000 was grown overnight in the KB medium and resuspended at 10⁸ ml in a solution of 10 mM MgCl₂ and 0.02% Silwet L-77. Two-week-old seedlings were dip inoculated with bacteria and kept covered for 1 h. The amount of bacteria in plants was analyzed at 1 h after dipping (day 0) and 3 days after dipping (day 3). The aerial parts of three inoculated seedlings were pooled for each sample and three samples were collected for each genotype at one time point. Seedlings were ground in 1 ml of 10 mM MgCl₂ and serial dilutions of ground tissue were used to determine the number of cfu per miligram of leaf tissues.

Engineering Heat-Stable Disease Resistance

As is discussed above, the invention involves engineering heat-stable disease resistance in plants where a heat-labile race-specific disease resistance is normally found. In general, mutant forms of an NB-LRR type of R protein that are responsible for this race-specific resistance are generated. Alternatively, mutant forms in natural populations are identified and isolated according to standard methods, followed by introducing such isolated R variants into plants, rendering such plants disease resistant against one or more pathogens at a temperature which would typically mask such a defense response.

Such R variants are useful to modify temperature sensitivity in disease resistance. Furthermore, R proteins may be altered at specific sites to generate an R protein which not only mediates disease resistance but one that is also heat-stable rendering a plant resistant to disease above its heat masking temperature.

As is also discussed above, the invention features methods for conferring disease resistance to a plant at a temperature at which such a disease response is suppressed, thereby attenuating heat masking. Such methods include, without limitation, overexpression or ectopic expression a heat-stable NB-LRR disease resistance polypeptide (such as SNC1-3, SNC1 E640R, N Y638K, N N640D, or N Y738K N640D or any polypeptide described in Appendix 4).

To test the ability of a construct described herein to confer disease resistance to a pathogen, transgenic plants expressing such construct are planted and disease resistance is compared to non-transformed plants using techniques familiar to those of skill in the art at masking temperatures. Plants expressing a heat-stable NB-LRR polypeptide have an “increased level of resistance” as compared to a control plant at the “masking temperature” of the control plant, and are taken as being useful in the invention. By “increased level of resistance” is meant a level of resistance to a disease-causing pathogen in a non-naturally occurring plant (or cell or seed thereof) which is greater than the level of resistance in a control plant (for example, a non-transgenic plant or wild-type or a transgenic plant or a wild-type plant with a heat-labile NB-LRR polypeptide). In preferred embodiments, the level of resistance in a non-naturally occurring transgenic plant of the invention is at least 5% to 20% (and preferably 30% or 40%) greater than the resistance exhibited by a control plant. In other preferred embodiments, the level of resistance to a disease-causing pathogen is 50% greater, 60% greater, and more preferably even 75% or 90% greater than a control plant; with up to 100% or greater above the level of resistance as compared to a control plant being most preferred. For example, a disease resistance response may be measured at 23° C., 24° C., 25° C., 26° C., 27° C., 28° C., 29° C., 30° C., 31° C., 32° C., 33° C., or greater relative to the masking temperature of a control plant which does not express a heat-stable NB-LRR disease resistance polypeptide. The level of resistance is measured using conventional methods such as those described herein. For example, the level of resistance to a pathogen may be determined by comparing physical features and characteristics (for example, plant height and weight) or by comparing disease symptoms (for example, delayed lesion development, reduced lesion size, leaf wilting and curling, water-soaked spots, amount of pathogen growth, and discoloration of cells) of the non-naturally occurring plant (e.g., a transgenic plant).

The invention also involves rendering heat-labile NB-LRR resistance genes heat-stable. This generally involves (1) identification of a heat-labile NB-LRR type of R gene, (2) Alignment of the protein sequence of Rs to those of SNC1 and N to identify LRR domain with identity to the heat-stability domain of SNC1; (3) Introduction of cognate mutations of snc1-3 into the Rs gene by site-directed mutagenesis; and (4) Assaying for temperature sensitivity.

1) Identification of the NB-LRR type of R gene responsible for resistance to a particular pathogen.

For heat-labile disease resistance, an R gene (referred to here as Rs) responsible for this resistance is identified. This is accomplished in a number of ways known in the art, for example, by map-based cloning exploring natural variations among different accessions of a plant species. Additional Rs genes are available in the art (See Appendices 1-3). Rs genes may also be identified in databases (See Appendices 1-3). Cloning and isolation of Rs is accomplished using standard methods known in the art.

2) Align the protein sequence of Rs to those of SNC1 and N and identify the corresponding residue of E640 of SNC1.

Most of the sequence analysis programs have a function for protein sequence alignment and they can all be used for this purpose. For instance, NCBI has ‘Blast 2’ for aligning two sequences and Vector NTI has an alignment function for two or more sequences. NB-LRR proteins have CC or TIR domains at the N-terminus, ARC-linker domains in the middle, and LRR domains at the C-terminus. The ARC-linker and LRR domains usually have high sequence similarities among different R proteins and are aligned easily.

3) Introduction of cognate mutations of snc1-3 into the Rs gene by site-directed mutagenesis.

The corresponding region of SNC1 640ELD in the Rs protein will be altered into KLD. This is achieved by site-directed mutagenesis kits available from a number of companies. For instance, ‘Quick-change’ from Invitrogen uses a complementary pair of primers with desired mutations a polymerase-chair reaction (PCR) to replace the wild-type sequences. The mutated Rs genes are sequenced to confirm that the desired mutations but not others are indeed introduced into the Rs protein.

4) Test the temperature sensitivity of the mutant Rs gene.

For those Rs genes where a transient assay for their activities are available (as for N and SNC1), the assay can be used to determine whether the mutant Rs gene confers disease resistance at a high temperature. Such an assay involves co-infiltrating the pathogen elicitor gene and the plant Rs gene into Nicotiana benthamiana through agrobacterium and monitoring hypersensitive responses (HR) at different temperatures. If the mutant Rs gene induces HR at high temperature while the wild-type Rs does not, the mutant gene indeed harbors the heat-stable property. If no such activity is achieved, a screen for such a mutation will be carried out as described below.

5) Isolate heat-stable mutations in the Rs gene

Random-mutagenesis is also used to create a mutant library of the Rs gene. This will be achieved through error-prone PCR or error-prone replication using Xl1-red cells. The DNA fragment coding for the linker and the LRR domains will be subject to such mutagenesis so that every fragment will have 0.1-0.5% of the nucleotides altered. These mutant fragments will be ligated with the rest of the Rs gene to reconstitute the full-length Rs genes. A library consisting of these mutated Rs genes will be screened for those that have HR causing activity at high temperatures described in step 4 above.

The invention also features the following:

1) Breed plants with heat-stable resistance

Variations in a plant species (either wild varieties or cultivars) provide resources for R gene variations. NB-LRR genes are the most rapidly evolved compared to other genes in Arabidopsis (37) and this is likely true in other plant species. It is possible that one particular variety has already evolved to harbor heat-stable disease resistance by evolving a mutation in the Rs gene. The invention accordingly provides a quick screen for such an R variant to assist plant breeding.

PCR is then used to amplify the linker and LRR regions of the Rs gene from different plant varieties. Rs genes with positively charged residues (K, R, or H) at the position corresponding to 640E in SNC1 are good candidate for variant conferring heat-stable resistance. These varieties can be tested directly for disease resistance at high temperatures.

Once the heat-stable resistance conferred by an Rs variant is found, this Rs variant will be introduced into crops by crossing the two varieties and isolating those with most of the elite traits together with the Rs variant in the F2 population with marker assisted selection.

Although the invention has been described in detail for the purpose of illustration, it is understood that such detail is solely for that purpose, and variations can be made therein by those skilled in the art without departing from the spirit and scope of the invention which is defined by the claims.

Other Embodiments

The invention provides methods of identifying, isolating, and using a nucleic acid molecule which encodes a NB-LRR disease resistant polypeptide which includes a heat-stable subdomain of the LRR.

A polypeptide that includes (a) a nucleotide binding (NB) domain and (b) a leucine rich repeat (LRR) domain, wherein the LRR domain includes a sub-domain that confers a heat-stable defense response to a plant pathogen includes variant polypeptides derived from a particular NB-LRR polypeptide by deletion (so-called truncation) or addition of one or more amino acids to the N-terminal and/or C-terminal end of the native protein; deletion or addition of one or more amino acids at one or more sites in the native protein; or substitution of one or more amino acids at one or more sites in the NB-LRR polypeptide. Such variants may result from, for example, from human manipulation. Methods for such manipulations are generally known in the art. For example, amino acid sequence variants of the polypeptides can be prepared by mutations in the DNA. Methods for mutagenesis and nucleotide sequence alterations are well known in the art. Guidance as to appropriate amino acid substitutions that do not affect biological activity of the protein of interest may be found in the art. Conservative substitutions, such as exchanging one amino acid with another having similar properties, are preferred.

Thus, the NB-LRR polypeptide genes and nucleotide sequences of the invention include both the naturally occurring sequences as well as mutant forms. Likewise, the NB-LRR polypeptides encompass both naturally occurring proteins as well as variations and modified forms thereof. Such variants will continue to possess the desired activity. The deletions, insertions, and substitutions of the NB-LRR polypeptide sequence encompassed herein are not expected to produce radical changes in the characteristics of the polypeptide. However, when it is difficult to predict the exact effect of the substitution, deletion, or insertion in advance of doing so, one skilled in the art will appreciate that the effect will be evaluated by routine screening assays such as those described herein.

The nucleic acid molecules are optimized for enhanced expression in plants. In this manner, the genes or gene fragments can be synthesized utilizing plant-preferred codons according to methods well known in the art. It is recognized that all or any part of the gene sequence may be optimized or synthetic. That is, synthetic or partially optimized sequences may also be used. Variant nucleotide sequences and proteins also encompass sequences and protein derived from a mutagenic and recombinant procedure such as DNA shuffling. With such a procedure, one or more different coding sequences can be manipulated to create a new polypeptide possessing the desired properties. In this manner, libraries of recombinant polynucleotides are generated from a population of related sequence polynucleotides comprising sequence regions that have substantial sequence identity and can be homologously recombined in vitro or in vivo. Strategies for such DNA shuffling are known in the art.

By “variants” is intended substantially similar sequences. For nucleotide sequences, variants include those sequences that, because of the degeneracy of the genetic code, encode the identical amino acid sequence of the reference protein. Naturally occurring allelic variants such as these can be identified with the use of well-known molecular biology techniques, as, for example, with polymerase chain reaction (PCR) and hybridization techniques. Variant nucleotide sequences also include synthetically derived nucleotide sequences, such as those generated, for example, by using site-directed mutagenesis which encode the reference protein, as well as those that encode a polypeptide having amino acid substitutions. Generally, nucleotide sequence variants of the invention will have at least 40%, 50%, 60%, preferably 70%, more preferably 80%, even more preferably 90%, most preferably 99%, and single unit percentage identity to the native nucleotide sequence based on these classes. For example, 40%, 41%, 42% and the like, up to at least the 90% class. Variants may also include a full length gene corresponding to an identified gene fragment.

Nucleic acid molecules which are substantially identical to any of the nucleic acid molecules described herein which encode NB-LRR polypeptides having a heat-stable LRR subdomain are included within the scope of the invention (for example, a SNC1-3, SNC1 E640R, N Y638K, N N640D, or N Y738K N640D polypeptide or any of the polypeptides described in Appendix 4).

By “substantially identical” is meant a polypeptide or nucleic acid exhibiting at least 40-50%, preferably 85%, more preferably 90%, and most preferably 95% homology to a reference amino acid or nucleic acid sequence. For polypeptides, the length of comparison sequences will generally be at least 16 amino acids, preferably at least 20 amino acids, more preferably at least 25 amino acids, and most preferably 35 amino acids. For nucleic acids, the length of comparison sequences will generally be at least 50 nucleotides, preferably at least 60 nucleotides, more preferably at least 75 nucleotides, and most preferably 110 nucleotides. Generally, nucleotide sequences will again have at least 40%, 50%, 60%, preferably 70%, more preferably 80%, even more preferably 90%, most preferably 99%, and single unit percentage identity to the NB-LRR nucleotide sequence (or polypeptide) based on these classes. For example, 40%, 41%, 42% and the like, up to at least the 90% class.

Sequence identity is typically measured using sequence analysis software (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis. 53705). Such software matches similar sequences by assigning degrees of homology to various substitutions, deletions, substitutions, and other modifications. Conservative substitutions typically include substitutions within the following groups: glycine alanine; valine, isoleucine, leucine; aspartic acid, glutamic acid, asparagine, glutamine; serine, threonine; lysine, arginine; and phenylalanine, tyrosine. For sequence comparison, typically one sequence acts as a reference sequence to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are input into a computer, subsequence coordinates are designated if necessary, and sequence algorithm program parameters are designated. The sequence comparison algorithm then calculates the percent sequence identity for the test sequence(s) relative to the reference sequence, based on the designated program parameters.

Plant cells useful in the invention as sources of nucleic acid molecules encoding heat-stable NB-LRR polypeptides as well as recipients for transformation using isolated nucleic acids molecules include preferably those with an agronomic, horticultural, ornamental, economic, or commercial value, and more preferably is include, without limitation, Acacia, alfalfa, apple, aneth, apple, apricot, artichoke, arugula, asparagus, avocado, balsam poplar, banana, barley, beans, beet, black cottonwood, blackberry, blueberry, broccoli, brussels sprouts, cabbage, canola, cantaloupe, carrot, cassava, castorbean, cauliflower, celery, cherry, chicory, cilantro, citrus, clementines, clover, coconut, coffee, corn, cotton, cucumber, Douglas fir, eggplant, endive, escarole, eucalyptus, fennel, figs, flax, French bean, garlic, gourd, grape, grapefruit, honey dew, Indian rice, Japanese rice, jicama, kiwifruit, lettuce, leeks, lemon, lime, Loblolly pine, linseed, mango, maize, melon, mushroom, nectarine, nut, oat, oil palm, oil seed rape, okra, olive, onion, orange, oriental melon, palm, papaya, parsley, parsnip, pea, peach, peanut, pear, pepper, persimmon, pine, pineapple, plantain, plum, pomegranate, poplar, potato, pumpkin, quince, radiata pine, radicchio, radish, rapeseed, raspberry, rice, rye, sorghum, Southern pine, soybean, spinach, squash, strawberry, sugarbeet, sugarcane, sunflower, sweet potato, sweetgum, tangerine, tea, tobacco, tomato, triticale, turf, turnip, a vine, watermelon, wheat, yams, and zucchini cell.

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APPENDICES Engineering Heat-Stable Plant Disease Resistance Via Modifying Disease Resistance Genes

More than 1000 proteins in protein database show homology to the SNC1 protein as Sep. 24, 2008. The list of homologs is shown in a taxa report in Appendix 1. The lists of homologs by their names are shown in Appendix 2 (for Arabidopsis thaliana) and Appendix 3 (for non-Arabidopsis thaliana). Each can be mutated to confer heat-stable disease resistance.

APPENDIX 1 A Taxa Report of SNC1 Homologs

It is generated by using the middle part of the SNC1 including the linker region and the first few LRR region (total 257 aa) as query to psi-Blast the non-redundant protein database for two iterations.

APPENDIX 2 List of SNC1 Homologs in Arabidopsis thaliana

A list of 500 homologous sequences of SNC1 found in Arabidopsis thaliana. There are more homologs as indicated in file 1, and only 500 can be shown in the Blast program result.

APPENDIX 3 List of SNC1 Homologs in Species Other than Arabidopsis thaliana

A list of 500 homologous sequences of SNC1 found in non-Arabidopsis thaliana species. There are more homologs as indicated in file 1, and only 500 can be shown in the Blast program result.

APPENDIX 4 R Mutations Useful for Conferring Heat-Stable Disease Resistance

A list of mutations in 27 R proteins useful for conferring heat-stable disease resistance. Shown are the name of the species, the name of the protein, and the mutations (in blue).

APPENDIX 1 A taxa report of SNC1 homologs Lineage Report cellular organisms  Embryophyta [land plants]   Spermatophyta [seed plants]    Magnoliophyta [flowering plants]     core eudicotyledons [eudicots]      rosids [eudicots]       Arabidopsis [eudicots]        Arabidopsis thaliana (thale-cress) 383 4019 hits [eudicots]        Arabidopsis lyrata (lyrate rockcress) 251 14 hits [eudicots]       Populus trichocarpa (black cottonwood) 346 83 hits [eudicots]       Cucumis melo (Oriental melon) 321 35 hits [eudicots]       Medicago sativa (alfalfa) 321 1 hit [eudicots]       Populus balsamifera (balsam poplar) 317 2 hits [eudicots]       Phaseolus vulgaris (French bean) 309 3 hits [eudicots]       Glycine max (soybeans) 306 54 hits [eudicots]       Medicago truncatula 304 25 hits [eudicots]       Malus baccata (shan jing si) 289 5 hits [eudicots]       Populus deltoides 281 3 hits [eudicots]       Lens culinaris 264 1 hit [eudicots]       Linum usitatissimum 219 179 hits [eudicots]       (Populus tomentosa × P. bolleana) × P. tomentosa var. truncata 208 2 hits [eudicots]       (Populus tomentosa × P. bolleana) × P. tomentosa 201 1 hit [eudicots]       Malus × domestics (cultivated apple) 101 1 hit [eudicots]      Vitis vinifera (wine grape) 374 682 hits [eudicots]      Solanum tuberosum (potatoes) 324 16 hits [eudicots]      Nicotiana tabacum (tobacco) 295 20 hits [eudicots]      Nicotiana glutinosa 278 8 hits [eudicots]      Solanum lycopersicum (tomato) 273 2 hits [eudicots]      Solanum tuberosum subsp. andigena 265 6 hits [eudicots]      Helianthus annuus 246 3 hits [eudicots]      Solanum demissum 172 6 hits [eudicots]      Vitis hybrid cultivar 87 3 hits [eudicots]     Orysa sativa Indica Group (Indian rice) 121 80 hits [monocots]     Orysa sativa Japonica Group (Japanese rice) 119 218 hits [monocots]     Hordeum vulgare (barley) 115 11 hits [monocots]     Zea mays (maize) 89 8 hits [monocots]    Pinus taeda 205 20 hits [conifers]    Picea sitchensis 115 4 hits [conifers]   Physcomitrella patens subsp. patens 155 840 hits [mosses] Summary of hits (homologous sequences found) Arabidopsis thaliana: 4019 black cottonwood: 83 oriental melon: 35 alfalfa: 1 balsam poplar: 2 French bean: 3 soybean: 54 flax: 179 apple: 1 wine grape: 682 potatoes: 16 tobacco: 20 tomato: 2 Indian rice: 80 Japanese rice: 218 barley: 11 maize: 8 Note: one gene may have more than one hit. In Arabidopsis thaliana, the average is about 2 hits per gene.

APPENDIX 2 List of SNC1 homologs in Arabidopsis thaliana Sequences producing significant alignments: (Bits) Value ref|NP_193422.1| SNC1 (SUPPRESSOR OF NPR1-1, CONSTITUTIVE 1) . . . 387 2e−107 ref|NP_851172.1| disease resistance protein (TIR-NBS-LRR clas . . . 340 3e−93 dbj|BAB08679.1| disease resistance protein; strong similarity . . . 339 5e−93 ref|NP_199976.2| disease resistance protein (TIR-NBS-LRR clas . . . 339 6e−93 gb|AAN86124.1| TIR-NBS-LRR [Arabidopsis thaliana] 333 2e−91 ref|NP_193428.2| RPP5 (RECOGNITION OF PERONOSPORA PARASITICA . . . 333 3e−91 ref|NP_849398.1| RPP5 (RECOGNITION OF PERONOSPORA PARASITICA . . . 332 6e−91 ref|NP_197298.1| disease resistance protein (TIR-NBS-LRR clas . . . 331 1e−90 emb|CAB46048.1| disease resistance RPP5 like protein [Arabido . . . 330 1e−90 pir||D71437 probable resistance gene - Arabidopsis thaliana 329 6e−90 ref|NP_198970.1| disease resistance protein (TIR-NBS-LRR clas . . . 328 8e−90 ref|NP_179279.1| disease resistance protein (TIR-NBS-LRR clas . . . 327 2e−89 ref|NP_200620.1| disease resistance protein (TIR-NBS-LRR clas . . . 326 4e−89 ref|NP_197337.1| disease resistance protein (TIR-NBS-LRR clas . . . 324 1e−88 ref|NP_197661.1| disease resistance protein (TIR-NBS-LRR clas . . . 324 1e−88 ref|NP_176571.1| disease resistance protein (TIR-NBS-LRR clas . . . 324 2e−88 ref|NP_198990.3| disease resistance protein (TIR-NBS-LRR clas . . . 322 5e−88 gb|AAG51270.1|AC027135_11 disease resistance gene, putative [. . . 322 6e−88 gb|AAG60157.1|AC074360_22 downy mildew resistance protein RPP . . . 322 7e−88 ref|NP_001117396.1| disease resistance protein (TIR-NBS-LRR c . . . 321 1e−87 ref|NP_174439.2| disease resistance protein (TIR-NBS-LRR clas . . . 321 1e−87 ref|NP_198907.1| disease resistance protein (TIR-NBS-LRR clas . . . 319 3e−87 ref|NP_199438.1| disease resistance protein (TIR-NBS-LRR clas . . . 319 3e−87 gb|AAS01763.1| TIR-NBS-LRR [Arabidopsis thaliana] 319 4e−87 gb|AAL36373.1| putative disease resistance protein [Arabidops . . . 317 2e−86 pir||B71437 probable resistance gene - Arabidopsis thaliana 317 2e−86 ref|NP_198969.1| disease resistance protein (TIR-NBS-LRR clas . . . 317 2e−86 emb|CAB10466.1| disease resistance RPP5 like protein [Arabido . . . 316 3e−86 gb|AAL91293.1| AT5g41750/MUF8_3 [Arabidopsis thaliana] >gb|AA . . . 316 3e−86 gb|AAL07075.1| putative disease resistance protein [Arabidops . . . 316 4e−86 ref|NP_199439.2| ATP binding/nucleoside-triphosphatase/nuc . . . 316 4e−86 dbj|BAB11082.1| disease resistance protein-like [Arabidopsis . . . 315 4e−86 ref|NP_192585.1| disease resistance protein (TIR-NBS-LRR clas . . . 315 7e−86 dbj|BAA97409.1| disease resistance protein-like [Arabidopsis . . . 315 8e−86 ref|NP_193425.1| disease resistance protein (TIR-NBS-LRR clas . . . 314 1e−85 dbj|BAA97354.1| disease resistance protein-like [Arabidopsis . . . 313 2e−85 dbj|BAC41800.2| putative disease resistance protein [Arabidop . . . 313 3e−85 dbj|BAB10815.1| disease resistance protein-like [Arabidopsis . . . 312 5e−85 emb|CAB43052.1| RPP1-WsA-like disease resistance protein [Ara . . . 312 5e−85 ref|NP_199457.1| disease resistance protein (TIR-NBS-LRR clas . . . 312 6e−85 ref|NP_198650.1| disease resistance protein (TIR-NBS-LRR clas . . . 312 6e−85 ref|NP_001077769.1| ATP binding/nucleoside-triphosphatase/ . . . 311 9e−85 gb|AAG52417.1|AC011622_5 putative disease resistance protein; . . . 311 1e−84 ref|NP_198651.1| disease resistance protein (NBS-LRR class), . . . 310 2e−84 ref|NP_199459.2| disease resistance protein (TIR-NBS-LRR clas . . . 310 2e−84 ref|NP_187072.1| disease resistance protein (TIR-NBS-LRR clas . . . 310 2e−84 ref|NP_176561.2| disease resistance protein (TIR-NBS-LRR clas . . . 309 3e−84 ref|NP_192855.1| disease resistance protein (TIR-NBS-LRR clas . . . 309 4e−84 gb|AAM20596.1| putative disease resistance protein [Arabidops . . . 309 4e−84 dbj|BAE98908.1| disease resistance like protein [Arabidopsis . . . 308 6e−84 ref|NP_001077768.1| ATP binding/nucleoside-triphosphatase/ . . . 308 7e−84 ref|NP_176560.1| disease resistance protein (TIR-NBS-LRR clas . . . 308 7e−84 dbj|BAC43641.2| putative disease resistance protein [Arabidop . . . 308 1e−83 ref|NP_176572.1| disease resistance protein (TIR-NBS-LRR clas . . . 307 1e−83 dbj|BAE98749.1| putative disease resistance protein [Arabidop . . . 307 1e−83 ref|NP_198701.1| disease resistance protein (TIR-NBS-LRR clas . . . 307 2e−83 ref|NP_189178.1| disease resistance protein (TIR-NBS-LRR clas . . . 306 4e−83 ref|NP_176760.2| disease resistance protein (TIR-NBS-LRR clas . . . 305 7e−83 ref|NP_179024.1| disease resistance protein (TIR-NBS-LRR clas . . . 304 1e−82 gb|AAM15274.1| disease resistance protein (TIR-NBS-LRR class) . . . 303 3e−82 dbj|BAB09567.1| disease resistance protein-like [Arabidopsis . . . 303 3e−82 ref|NP_197270.1| disease resistance protein (TIR-NBS-LRR clas . . . 303 3e−82 dbj|BAB10522.1| disease resistance protein-like [Arabidopsis . . . 303 3e−82 ref|NP_193173.1| disease resistance protein (TIR-NBS-LRR clas . . . 300 2e−81 emb|CAB10461.1| disease resistance RPP5 like protein [Arabido . . . 300 3e−81 ref|NP_199264.1| disease resistance protein (TIR-NBS-LRR clas . . . 299 3e−81 gb|ABS82020.1| TAO1 [Arabidopsis thaliana] 298 6e−81 gb|ABS82021.1| TAO1 [Arabidopsis thaliana] 298 1e−80 gb|AAM18462.1| AF440696_1 disease resistance protein RPP4 [Ara . . . 298 1e−80 ref|NP_199725.1| disease resistance protein (TIR-NBS-LRR clas . . . 294 1e−79 ref|NP_197338.1| disease resistance protein (TIR-NBS-LRR clas . . . 294 1e−79 ref|NP_196686.1| disease resistance protein (TIR-NBS-LRR clas . . . 293 2e−79 ref|NP_199463.1| disease resistance protein (TIR-NBS-LRR clas . . . 293 2e−79 ref|NP_193420.2| RPP4 (RECOGNITION OF PERONOSPORA PARASITICA . . . 293 3e−79 emb|CAB80962.1| disease resistance RPP5 like protein [Arabido . . . 293 4e−79 gb|AAF24575.1|AC007764_17 F22C12.17 [Arabidopsis thaliana] 292 4e−79 ref|NP_176047.1| disease resistance protein (TIR-NBS-LRR clas . . . 292 4e−79 dbj|BAB10820.1| disease resistance protein-like [Arabidopsis . . . 292 8e−79 gb|AAM53313.1| disease resistance RPP5-like protein [Arabidop . . . 291 9e−79 ref|NP_199464.2| ATP binding/nucleoside-triphosphatase/nuc . . . 291 1e−78 gb|AAG60098.1|AC073178_9 disease resistance protein, putative . . . 291 1e−78 dbj|BAE98880.1| disease resistance like protein [Arabidopsis . . . 290 3e−78 ref|NP_193424.2| ATP binding/protein binding/transmembran . . . 289 3e−78 ref|NP_176590.2| RLM1 (RESISTANCE TO LEPTOSPHAERIA MACULANS 1 . . . 289 5e−78 ref|NP_197336.1| disease resistance protein (TIR-NBS-LRR clas . . . 288 6e−78 gb|AAM97118.1| disease resistance protein-like [Arabidopsis t . . . 287 1e−77 gb|AAC72978.1| disease resistance protein RPP1-WsB [Arabidops . . . 287 2e−77 ref|NP_198989.2| disease resistance protein (TIR-NBS-LRR clas . . . 286 3e−77 dbj|BAE99086.1| disease resistance like protein [Arabidopsis . . . 286 3e−77 ref|NP_192939.2| WRKY19 (WRKY DNA-binding protein 19); transc . . . 286 4e−77 ref|NP_001118968.1| WRKY19 (WRKY DNA-binding protein 19) [Ara . . . 285 6e−77 dbj|BAE98800.1| hypothetical protein [Arabidopsis thaliana] 283 2e−76 ref|NP_176043.1| disease resistance protein (TIR-NBS-LRR clas . . . 283 3e−76 gb|AAC72977.1| disease resistance protein RPP1-WsA [Arabidops . . . 282 5e−76 emb|CAB88530.1| disease resistance protein-like [Arabidopsis . . . 279 5e−75 gb|AAG09110.1|AC009323_21 Putative disease resistance protein . . . 278 7e−75 ref|NP_190034.2| RPP1 (RECOGNITION OF PERONOSPORA PARASITICA . . . 278 8e−75 ref|NP_176044.1| disease resistance protein (TIR-NBS-LRR clas . . . 278 8e−75 gb|AAF08790.1| downy mildew resistance protein RPP5 [Arabidop . . . 278 1e−74 ref|NP_193427.1| disease resistance protein (TIR-NBS-LRR clas . . . 277 1e−74 ref|NP_001078237.1| ATP binding/nucleoside-triphosphatase/ . . . 277 2e−74 dbj|BAD94052.1| disease resistance - like protein [Arabidopsi . . . 277 2e−74 emb|CAB72469.1| disease resistance protein homlog [Arabidopsi . . . 277 2e−74 ref|NP_190026.1| disease resistance protein (TIR-NBS-LRR clas . . . 277 2e−74 gb|AAC72979.1| disease resistance protein RPP1-WsC [Arabidops . . . 273 3e−73 gb|AAM13214.1| disease resistance protein-like [Arabidopsis t . . . 270 3e−72 ref|NP_192938.1| disease resistance protein (TIR-NBS-LRR clas . . . 268 8e−72 gb|AAR92462.1| SNC1-like protein [Arabidopsis thaliana] 268 1e−71 dbj|BAC42557.1| putative disease resistance protein [Arabidop . . . 267 2e−71 gb|ABB00837.1| disease resistance protein [Arabidopsis thalia . . . 264 2e−70 gb|ABB00835.1| disease resistance protein [Arabidopsis thalia . . . 263 3e−70 gb|ABB00834.1| disease resistance protein [Arabidopsis thaliana] 261 1e−69 gb|ABB00838.1| disease resistance protein [Arabidopsis thaliana] 261 1e−69 ref|NP_193685.3| disease resistance protein (TIR-NBS-LRR clas . . . 261 1e−69 ref|NP_199338.1| RPS4 (RESISTANT TO P. SYRINGAE 4) [Arabidops . . . 261 2e−69 gb|ABB00836.1| disease resistance protein [Arabidopsis thaliana] 261 2e−69 emb|CAB53784.1| disease resistance protein rps4-RLD [Arabidop . . . 260 2e−69 emb|CAA16927.2| resistence protein-like [Arabidopsis thaliana . . . 260 3e−69 emb|CAB53785.1| disease resistance protein RPS4-Ler [Arabidop . . . 259 4e−69 ref|NP_176078.1| disease resistance protein (NBS-LRR class), . . . 258 9e−69 dbj|BAB01321.1| disease resistance protein RPP1-WsB [Arabidop . . . 257 2e−68 gb|ABB00841.1| disease resistance protein [Arabidopsis lyrata] 257 2e−68 emb|CAA16928.1| TMV resistance protein N-like [Arabidopsis th . . . 255 7e−68 ref|NP_193686.2| disease resistance protein (TIR-NBS-LRR clas . . . 255 8e−68 dbj|BAF01192.1| resistence protein - like [Arabidopsis thaliana] 255 9e−68 dbj|BAB11393.1| disease resistance protein RPS4 [Arabidopsis . . . 250 2e−66 ref|NP_199333.1| disease resistance protein (TIR-NBS-LRR clas . . . 250 2e−66 ref|NP_177427.2| ATP binding/protein binding/transmembran . . . 250 3e−66 ref|NP_193429.1| disease resistance protein (TIR-NBS-LRR clas . . . 250 3e−66 ref|NP_197290.1| CSA1 (CONSTITUTIVE SHADE-AVOIDANCE1); ATP bi . . . 249 5e−66 ref|NP_199319.1| disease resistance protein (TIR-NBS-LRR clas . . . 248 7e−66 dbj|BAB11221.1| disease resistance protein [Arabidopsis thali . . . 248 7e−66 ref|NP_199300.1| disease resistance protein (TIR-NBS-LRR clas . . . 243 2e−64 ref|NP_199318.2| TTR1 (WRKY domain family protein 16); transc . . . 243 4e−64 ref|NP_190049.1| disease resistance protein RPP1-WsB-like (TI . . . 242 6e−64 ref|NP_190725.1| disease resistance protein (TIR-NBS-LRR clas . . . 242 7e−64 ref|NP_195338.1| disease resistance protein (TIR-NBS-LRR clas . . . 241 2e−63 ref|NP_850655.1| disease resistance protein RPP1-WsB-like (TI . . . 240 2e−63 ref|NP_851133.1| TTR1 (WRKY domain family protein 16); transc . . . 240 2e−63 ref|NP_199688.1| disease resistance protein (TIR-NBS-LRR clas . . . 238 7e−63 ref|NP_195337.1| disease resistance protein (TIR-NBS-LRR clas . . . 238 1e−62 gb|AAO45748.1| MRGH5 [Cucumis melo] 237 3e−62 ref|NP_198509.2| disease resistance protein (TIR-NBS-LRR clas . . . 232 6e−61 ref|NP_001119319.1| disease resistance protein (TIR-NBS-LRR c . . . 232 7e−61 dbj|BAB11635.1| TMV resistance protein N [Arabidopsis thaliana] 232 8e−61 ref|NP_193688.1| disease resistance protein (TIR-NBS-LRR clas . . . 231 1e−60 ref|NP_179297.2| disease resistance protein (TIR-NBS-LRR clas . . . 230 3e−60 dbj|BAD38678.1| disease resistance protein SLH1 [Arabidopsis . . . 229 5e−60 gb|AAF18599.1|AC002354_8 putative disease resistance protein . . . 228 8e−60 ref|NP_199339.2| RRS1 (RESISTANT TO RALSTONIA SOLANACEARUM 1) . . . 227 3e−59 ref|NP_199336.1| disease resistance protein (TIR-NBS-LRR clas . . . 226 3e−59 ref|NP_199334.1| disease resistance protein (TIR-NBS-LRR clas . . . 226 5e−59 dbj|BAC41834.1| putative disease resistance protein [Arabidop . . . 225 1e−58 ref|NP_001078715.1| RRS1 (RESISTANT TO RALSTONIA SOLANACEARUM . . . 225 1e−58 gb|AAO45749.1| MRGH63 [Cucumis melo] 222 6e−58 gb|AAD55631.1|AC008017_4 Similar to disease resistance protei . . . 218 1e−56 ref|NP_190724.1| disease resistance protein (TIR-NBS-LRR clas . . . 218 1e−56 dbj|BAB11222.1| disease resistance protein-like [Arabidopsis . . . 213 3e−55 dbj|BAE99034.1| disease resistance RPP5 like protein [Arabido . . . 213 3e−55 ref|NP_197291.2| LIM domain-containing protein/disease resi . . . 213 5e−55 gb|AAG13419.1|AC000348_16 T7N9.24 [Arabidopsis thaliana] 212 6e−55 ref|NP_174038.1| disease resistance protein (TIR-NBS-LRR clas . . . 211 9e−55 ref|NP_174037.3| ATP binding/protein binding/transmembran . . . 209 4e−54 ref|NP_179298.2| disease resistance protein (TIR-NBS-LRR clas . . . 209 5e−54 gb|AAF18600.1|AC002354_9 putative disease resistance protein . . . 208 8e−54 ref|NP_974894.1| disease resistance protein (TIR-NBS class), . . . 206 4e−53 gb|AAF79477.1|AC022492_21 F1L3.30 [Arabidopsis thaliana] 203 2e−52 ref|NP_173203.1| disease resistance protein (TIR-NBS-LRR clas . . . 201 9e−52 gb|AAG13418.1|AC000348_15 T7N9.23 [Arabidopsis thaliana] 199 5e−51 emb|CAA16929.1| resistance protein RPP5-like [Arabidopsis tha . . . 198 1e−50 ref|NP_564971.1| disease resistance protein (TIR-NBS class), . . . 198 1e−50 ref|NP_177429.2| disease resistance protein (TIR-NBS-LRR clas . . . 194 1e−49 ref|NP_193687.2| disease resistance protein (TIR-NBS-LRR clas . . . 191 1e−48 gb|ABG01388.1| disease resistance protein [Arabidopsis thaliana] 190 3e−48 gb|ABG01367.1| disease resistance protein [Arabidopsis thaliana] 188 9e−48 gb|ABG01389.1| disease resistance protein [Arabidopsis thalia . . . 188 1e−47 gb|ABG01364.1| disease resistance protein [Arabidopsis thalia . . . 188 1e−47 gb|ABG01435.1| disease resistance protein [Arabidopsis thaliana] 188 1e−47 gb|ABG01423.1| disease resistance protein [Arabidopsis thaliana] 188 2e−47 gb|ABG01408.1| disease resistance protein [Arabidopsis thalia . . . 187 2e−47 gb|ABG01361.1| disease resistance protein [Arabidopsis thalia . . . 187 2e−47 gb|ABG01393.1| disease resistance protein [Arabidopsis thalia . . . 187 2e−47 gb|ABG01372.1| disease resistance protein [Arabidopsis thalia . . . 187 2e−47 gb|ABG01366.1| disease resistance protein [Arabidopsis thalia . . . 187 2e−47 gb|ABG01369.1| disease resistance protein [Arabidopsis thaliana] 186 3e−47 gb|ABG01362.1| disease resistance protein [Arabidopsis thalia . . . 186 4e−47 gb|ABF74126.1| disease resistance protein [Arabidopsis thaliana] 186 4e−47 gb|ABF74127.1| disease resistance protein [Arabidopsis thaliana] 186 4e−47 gb|ABG01434.1| disease resistance protein [Arabidopsis thaliana] 186 4e−47 gb|ABG01419.1| disease resistance protein [Arabidopsis thaliana] 186 5e−47 gb|ABF74109.1| disease resistance protein [Arabidopsis thaliana] 186 5e−47 gb|ABF74098.1| disease resistance protein [Arabidopsis thaliana] 186 5e−47 gb|ABG01383.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74119.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74139.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74087.1| disease resistance protein [Arabidopsis thalia . . . 186 6e−47 gb|ABF74125.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74136.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74106.1| disease resistance protein [Arabidopsis thaliana] 186 6e−47 gb|ABF74111.1| disease resistance protein [Arabidopsis thaliana] 185 7e−47 gb|ABG01395.1| disease resistance protein [Arabidopsis thalia . . . 185 8e−47 gb|ABG01410.1| disease resistance protein [Arabidopsis thaliana] 185 8e−47 gb|ABF74124.1| disease resistance protein [Arabidopsis thaliana] 185 9e−47 gb|ABF74086.1| disease resistance protein [Arabidopsis thalia . . . 185 9e−47 gb|ABF74133.1| disease resistance protein [Arabidopsis thalia . . . 185 9e−47 gb|ABG01439.1| disease resistance protein [Arabidopsis thaliana] 185 9e−47 gb|ABG01422.1| disease resistance protein [Arabidopsis thaliana] 185 1e−46 gb|ABF74089.1| disease resistance protein [Arabidopsis thalia . . . 185 1e−46 gb|ABF74116.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABG01375.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABF74110.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABG01418.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABF74093.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABF74140.1| disease resistance protein [Arabidopsis thaliana] 184 1e−46 gb|ABG01370.1| disease resistance protein [Arabidopsis thaliana] 184 2e−46 gb|ABF74092.1| disease resistance protein [Arabidopsis thalia . . . 184 2e−46 gb|ABF74123.1| disease resistance protein [Arabidopsis thaliana] 184 2e−46 gb|ABF74129.1| disease resistance protein [Arabidopsis thaliana] 184 2e−46 gb|ABF74112.1| disease resistance protein [Arabidopsis thalia . . . 184 2e−46 gb|ABF74117.1| disease resistance protein [Arabidopsis thaliana] 184 2e−46 ref|NP_192681.1| disease resistance protein (TIR-NBS-LRR clas . . . 183 3e−46 gb|ABG01399.1| disease resistance protein [Arabidopsis thalia . . . 183 3e−46 gb|ABG01384.1| disease resistance protein [Arabidopsis thalia . . . 183 3e−46 gb|ABG01426.1| disease resistance protein [Arabidopsis thaliana] 183 3e−46 gb|ABF74122.1| disease resistance protein [Arabidopsis thaliana] 183 4e−46 gb|ABG01368.1| disease resistance protein [Arabidopsis thaliana] 183 5e−46 gb|ABG01430.1| disease resistance protein [Arabidopsis thaliana] 183 5e−46 gb|ABF74095.1| disease resistance protein [Arabidopsis thaliana] 182 7e−46 ref|NP_198826.1| disease resistance protein (TIR-NBS-LRR clas . . . 182 8e−46 gb|ABG01412.1| disease resistance protein [Arabidopsis thaliana] 181 1e−45 gb|ABG01420.1| disease resistance protein [Arabidopsis thaliana] 174 2e−43 dbj|BAB09118.1| unnamed protein product [Arabidopsis thaliana] 174 2e−43 gb|ABG01407.1| disease resistance protein [Arabidopsis thaliana] 170 3e−42 gb|AAD55633.1|AC008017_6 Similar to downy mildew resistance p . . . 161 2e−39 dbj|BAF01370.1| disease resistance like protein [Arabidopsis . . . 159 6e−39 gb|ABG00946.1| disease resistance protein [Arabidopsis thalia . . . 149 6e−36 gb|ABG00949.1| disease resistance protein [Arabidopsis thalia . . . 149 6e−36 gb|ABG01024.1| disease resistance protein [Arabidopsis thaliana] 149 6e−36 gb|ABG01022.1| disease resistance protein [Arabidopsis thaliana] 149 9e−36 gb|ABG01034.1| disease resistance protein [Arabidopsis thaliana] 148 1e−35 gb|ABG01044.1| disease resistance protein [Arabidopsis thalia . . . 148 1e−35 gb|ABG01119.1| disease resistance protein [Arabidopsis thaliana] 148 1e−35 gb|ABG01036.1| disease resistance protein [Arabidopsis thalia . . . 148 1e−35 gb|ABG00991.1| disease resistance protein [Arabidopsis thaliana] 147 2e−35 gb|ABG01043.1| disease resistance protein [Arabidopsis thalia . . . 147 2e−35 gb|ABG01041.1| disease resistance protein [Arabidopsis thalia . . . 147 2e−35 gb|ABG01039.1| disease resistance protein [Arabidopsis thalia . . . 147 2e−35 gb|ABG01058.1| disease resistance protein [Arabidopsis thalia . . . 147 2e−35 gb|ABG01076.1| disease resistance protein [Arabidopsis thaliana] 147 2e−35 gb|ABG01050.1| disease resistance protein [Arabidopsis thalia . . . 147 2e−35 gb|ABG00983.1| disease resistance protein [Arabidopsis thaliana] 147 3e−35 gb|ABG01006.1| disease resistance protein [Arabidopsis thaliana] 146 5e−35 gb|ABG00998.1| disease resistance protein [Arabidopsis thaliana] 146 7e−35 gb|ABG01094.1| disease resistance protein [Arabidopsis thaliana] 145 9e−35 gb|ABG00988.1| disease resistance protein [Arabidopsis thalia . . . 145 1e−34 gb|AAD25848.3| disease resistance protein (TIR-NBS-LRR class) . . . 134 1e−31 ref|NP_193421.2| disease resistance protein-related [Arabidop . . . 134 2e−31 ref|NP_001045334.1| Os01g0937300 [Oryza sativa (japonica cult . . . 134 3e−31 emb|CAB10464.1| disease resistance RPP5 like protein (fragmen . . . 133 4e−31 ref|NP_683486.1| leucine-rich repeat family protein [Arabidop . . . 133 5e−31 gb|ABG01208.1| disease resistance protein [Arabidopsis thaliana] 133 5e−31 gb|ABG01201.1| disease resistance protein [Arabidopsis thalia . . . 132 6e−31 gb|ABG01205.1| disease resistance protein [Arabidopsis thalia . . . 132 7e−31 gb|ABG01197.1| disease resistance protein [Arabidopsis thalia . . . 132 8e−31 gb|ABG01248.1| disease resistance protein [Arabidopsis thaliana] 132 8e−31 gb|ABG01209.1| disease resistance protein [Arabidopsis thalia . . . 131 1e−30 gb|ABF73632.1| disease resistance protein [Arabidopsis thaliana] 130 4e−30 gb|ABF73595.1| disease resistance protein [Arabidopsis thalia . . . 130 4e−30 gb|ABF73596.1| disease resistance protein [Arabidopsis thaliana] 130 4e−30 gb|ABF73641.1| disease resistance protein [Arabidopsis thaliana] 129 4e−30 dbj|BAF01484.1| disease resistance RPP5 like protein [Arabido . . . 129 5e−30 gb|ABF73605.1| disease resistance protein [Arabidopsis thalia . . . 129 6e−30 gb|ABF73590.1| disease resistance protein [Arabidopsis thalia . . . 129 6e−30 gb|ABF73604.1| disease resistance protein [Arabidopsis thaliana] 129 6e−30 gb|ABF73616.1| disease resistance protein [Arabidopsis thalia . . . 129 6e−30 gb|ABF73617.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73623.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73639.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73603.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73599.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73619.1| disease resistance protein [Arabidopsis thaliana] 128 1e−29 gb|ABF73649.1| disease resistance protein [Arabidopsis thaliana] 128 2e−29 gb|ABF74258.1| disease resistance protein [Arabidopsis thalia . . . 128 2e−29 gb|ABF73612.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABF73654.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABF73591.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABF73660.1| disease resistance protein [Arabidopsis thaliana] 127 2e−29 gb|ABF74233.1| disease resistance protein [Arabidopsis thaliana] 127 2e−29 gb|ABF73673.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABG01607.1| disease resistance protein [Arabidopsis thaliana] 127 2e−29 gb|ABF73602.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABF73588.1| disease resistance protein [Arabidopsis thalia . . . 127 2e−29 gb|ABF73634.1| disease resistance protein [Arabidopsis thaliana] 127 2e−29 gb|ABF73597.1| disease resistance protein [Arabidopsis thaliana] 127 3e−29 gb|ABG01548.1| disease resistance protein [Arabidopsis thalia . . . 127 3e−29 gb|ABF73621.1| disease resistance protein [Arabidopsis thaliana] 127 3e−29 gb|ABF73611.1| disease resistance protein [Arabidopsis thaliana] 127 3e−29 gb|ABF74263.1| disease resistance protein [Arabidopsis thalia . . . 127 4e−29 gb|ABG01574.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABF74292.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABG01661.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABG01561.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABF73633.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABG01575.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABG01581.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABG01537.1| disease resistance protein [Arabidopsis thaliana] 126 4e−29 gb|ABF73626.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABF74221.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABF73659.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABG01583.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABG01593.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABG01555.1| disease resistance protein [Arabidopsis thalia . . . 126 5e−29 gb|ABG01536.1| disease resistance protein [Arabidopsis thalia . . . 126 5e−29 gb|ABG01535.1| disease resistance protein [Arabidopsis thalia . . . 126 5e−29 gb|ABF74295.1| disease resistance protein [Arabidopsis thaliana] 126 5e−29 gb|ABF74248.1| disease resistance protein [Arabidopsis thalia . . . 126 5e−29 gb|ABF74282.1| disease resistance protein [Arabidopsis thaliana] 126 6e−29 gb|ABF74224.1| disease resistance protein [Arabidopsis thalia . . . 126 6e−29 gb|ABF74241.1| disease resistance protein [Arabidopsis thalia . . . 126 6e−29 gb|ABF74235.1| disease resistance protein [Arabidopsis thaliana] 126 6e−29 gb|ABF73625.1| disease resistance protein [Arabidopsis thaliana] 126 6e−29 gb|ABG01599.1| disease resistance protein [Arabidopsis thalia . . . 126 7e−29 gb|ABF73598.1| disease resistance protein [Arabidopsis thalia . . . 126 7e−29 gb|ABG01585.1| disease resistance protein [Arabidopsis thaliana] 126 7e−29 gb|ABF73618.1| disease resistance protein [Arabidopsis thaliana] 126 7e−29 gb|ABF73640.1| disease resistance protein [Arabidopsis thalia . . . 126 7e−29 gb|ABF73608.1| disease resistance protein [Arabidopsis thaliana] 126 7e−29 gb|ABF73678.1| disease resistance protein [Arabidopsis thaliana] 126 7e−29 gb|ABF73607.1| disease resistance protein [Arabidopsis thaliana] 126 7e−29 gb|ABF74281.1| disease resistance protein [Arabidopsis thaliana] 126 8e−29 gb|ABF74220.1| disease resistance protein [Arabidopsis thaliana] 126 8e−29 gb|ABF74232.1| disease resistance protein [Arabidopsis thaliana] 126 8e−29 gb|ABG01619.1| disease resistance protein [Arabidopsis thaliana] 126 8e−29 gb|ABG01628.1| disease resistance protein [Arabidopsis thaliana] 126 8e−29 gb|ABF74226.1| disease resistance protein [Arabidopsis thalia . . . 125 8e−29 gb|ABF74231.1| disease resistance protein [Arabidopsis thaliana] 125 8e−29 gb|ABG01538.1| disease resistance protein [Arabidopsis thaliana] 125 8e−29 gb|ABG01533.1| disease resistance protein [Arabidopsis thalia . . . 125 9e−29 gb|ABG01551.1| disease resistance protein [Arabidopsis thaliana] 125 9e−29 gb|ABG01648.1| disease resistance protein [Arabidopsis thaliana] 125 9e−29 gb|ABG01639.1| disease resistance protein [Arabidopsis thaliana] 125 9e−29 gb|ABG01562.1| disease resistance protein [Arabidopsis thalia . . . 125 9e−29 gb|ABG01600.1| disease resistance protein [Arabidopsis thalia . . . 125 9e−29 gb|ABG01677.1| disease resistance protein [Arabidopsis thalia . . . 125 1e−28 gb|ABG01553.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01541.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01554.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF73609.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01531.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF74246.1| disease resistance protein [Arabidopsis thalia . . . 125 1e−28 gb|ABG01540.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01591.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01556.1| disease resistance protein [Arabidopsis thalia . . . 125 1e−28 gb|ABG01569.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF74222.1| disease resistance protein [Arabidopsis thalia . . . 125 1e−28 gb|ABG01622.1| disease resistance protein [Arabidopsis thalia . . . 125 1e−28 gb|ABF73664.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF73589.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF73675.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01567.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01594.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABF73635.1| disease resistance protein [Arabidopsis thaliana] 125 1e−28 gb|ABG01601.1| disease resistance protein [Arabidopsis thalia . . . 124 1e−28 gb|ABF73657.1| disease resistance protein [Arabidopsis thaliana] 124 1e−28 gb|ABG01557.1| disease resistance protein [Arabidopsis thaliana] 124 2e−28 gb|ABG01552.1| disease resistance protein [Arabidopsis thaliana] 124 2e−28 gb|ABF74227.1| disease resistance protein [Arabidopsis thaliana] 124 3e−28 gb|ABF73594.1| disease resistance protein [Arabidopsis thalia . . . 124 3e−28 gb|ABG01588.1| disease resistance protein [Arabidopsis thaliana] 124 3e−28 gb|ABF74287.1| disease resistance protein [Arabidopsis thaliana] 124 3e−28 gb|ABF73593.1| disease resistance protein [Arabidopsis thaliana] 123 3e−28 gb|ABG01532.1| disease resistance protein [Arabidopsis thaliana] 123 3e−28 gb|ABG01584.1| disease resistance protein [Arabidopsis thaliana] 123 3e−28 gb|ABF74291.1| disease resistance protein [Arabidopsis thaliana] 123 3e−28 gb|ABG01590.1| disease resistance protein [Arabidopsis thaliana] 123 3e−28 gb|ABG01543.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABF73638.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABG01587.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABF73601.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABF73606.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABG01658.1| disease resistance protein [Arabidopsis thaliana] 123 4e−28 gb|ABF73671.1| disease resistance protein [Arabidopsis thaliana] 123 5e−28 gb|ABG01586.1| disease resistance protein [Arabidopsis thaliana] 122 9e−28 gb|ABF73655.1| disease resistance protein [Arabidopsis thaliana] 122 1e−27 gb|ABG01589.1| disease resistance protein [Arabidopsis thaliana] 122 1e−27 gb|ABG01579.1| disease resistance protein [Arabidopsis thaliana] 121 1e−27 gb|ABG01559.1| disease resistance protein [Arabidopsis thaliana] 121 1e−27 gb|ABB00875.1| disease resistance protein [Arabidopsis thalia . . . 118 1e−26 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica cult . . . 118 1e−26 gb|ABB00889.1| disease resistance protein [Arabidopsis thaliana] 118 1e−26 gb|ABF73725.1| disease resistance protein [Arabidopsis thalia . . . 117 2e−26 gb|ABF73684.1| disease resistance protein [Arabidopsis thalia . . . 117 2e−26 gb|ABF73729.1| disease resistance protein [Arabidopsis thaliana] 117 2e−26 gb|ABF73682.1| disease resistance protein [Arabidopsis thalia . . . 117 3e−26 gb|ABF73721.1| disease resistance protein [Arabidopsis thaliana] 117 3e−26 gb|ABF73732.1| disease resistance protein [Arabidopsis thaliana] 117 3e−26 gb|ABF73686.1| disease resistance protein [Arabidopsis thaliana] 117 3e−26 gb|ABF73755.1| disease resistance protein [Arabidopsis thaliana] 117 3e−26 gb|ABF73722.1| disease resistance protein [Arabidopsis thaliana] 117 4e−26 gb|ABF73679.1| disease resistance protein [Arabidopsis thalia . . . 116 4e−26 gb|ABF73694.1| disease resistance protein [Arabidopsis thaliana] 116 4e−26 gb|ABF73670.1| disease resistance protein [Arabidopsis thaliana] 116 6e−26 gb|ABF73681.1| disease resistance protein [Arabidopsis thalia . . . 116 6e−26 gb|ABF73698.1| disease resistance protein [Arabidopsis thaliana] 116 7e−26 gb|ABF73720.1| disease resistance protein [Arabidopsis thaliana] 116 7e−26 gb|ABF73742.1| disease resistance protein [Arabidopsis thaliana] 115 9e−26 gb|ABF73718.1| disease resistance protein [Arabidopsis thaliana] 115 1e−25 gb|ABF73680.1| disease resistance protein [Arabidopsis thaliana] 115 1e−25 gb|ABF73719.1| disease resistance protein [Arabidopsis thaliana] 114 2e−25 gb|ABF73449.1| disease resistance protein [Arabidopsis thalia . . . 114 2e−25 gb|ABF73439.1| disease resistance protein [Arabidopsis thalia . . . 114 2e−25 gb|ABF74253.1| disease resistance protein [Arabidopsis thalia . . . 114 2e−25 gb|ABF74294.1| disease resistance protein [Arabidopsis thaliana] 114 2e−25 gb|ABF73703.1| disease resistance protein [Arabidopsis thalia . . . 114 3e−25 gb|ABF73422.1| disease resistance protein [Arabidopsis thalia . . . 114 3e−25 gb|ABF73429.1| disease resistance protein [Arabidopsis thalia . . . 114 3e−25 gb|ABF73436.1| disease resistance protein [Arabidopsis thaliana] 113 4e−25 gb|ABF73493.1| disease resistance protein [Arabidopsis thaliana] 113 4e−25 gb|ABF73466.1| disease resistance protein [Arabidopsis thalia . . . 113 4e−25 gb|ABF73424.1| disease resistance protein [Arabidopsis thalia . . . 113 4e−25 gb|ABF73434.1| disease resistance protein [Arabidopsis thaliana] 113 5e−25 gb|ABF73459.1| disease resistance protein [Arabidopsis thaliana] 112 6e−25 gb|ABF73423.1| disease resistance protein [Arabidopsis thalia . . . 112 7e−25 gb|ABF73425.1| disease resistance protein [Arabidopsis thalia . . . 112 9e−25 gb|ABF73430.1| disease resistance protein [Arabidopsis thalia . . . 112 1e−24 gb|ABF73467.1| disease resistance protein [Arabidopsis thaliana] 111 1e−24 gb|ABF73485.1| disease resistance protein [Arabidopsis thaliana] 111 2e−24 gb|ABF73490.1| disease resistance protein [Arabidopsis thalia . . . 110 2e−24 gb|ABB00900.1| disease resistance protein [Arabidopsis lyrata] 110 2e−24 ref|NP_001043262.1| Os01g0536600 [Oryza sativa (japonica cult . . . 110 2e−24 ref|NP_199337.2| disease resistance protein (TIR-NBS-LRR clas . . . 110 3e−24 ref|NP_001062892.1| Os09g0327800 [Oryza sativa (japonica cult . . . 110 3e−24 gb|ABG01153.1| disease resistance protein [Arabidopsis thaliana] 110 4e−24 gb|ABG01121.1| disease resistance protein [Arabidopsis thalia . . . 109 5e−24 gb|EAZ08636.1| hypothetical protein OsI_029868 [Oryza sativa . . . 109 5e−24 gb|ABG01191.1| disease resistance protein [Arabidopsis thaliana] 109 5e−24 gb|ABG01188.1| disease resistance protein [Arabidopsis thaliana] 109 5e−24 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica cult . . . 109 5e−24 gb|ABG00706.1| disease resistance protein [Arabidopsis thalia . . . 109 6e−24 gb|ABG00698.1| disease resistance protein [Arabidopsis thaliana] 109 6e−24 gb|ABG00693.1| disease resistance protein [Arabidopsis thalia . . . 109 7e−24 gb|ABG00690.1| disease resistance protein [Arabidopsis thalia . . . 109 7e−24 gb|ABG00724.1| disease resistance protein [Arabidopsis thalia . . . 109 7e−24 gb|ABG00691.1| disease resistance protein [Arabidopsis thalia . . . 109 7e−24 gb|ABG00719.1| disease resistance protein [Arabidopsis thalia . . . 109 7e−24 dbj|BAB10245.1| unnamed protein product [Arabidopsis thaliana] 109 8e−24 gb|ABG00697.1| disease resistance protein [Arabidopsis thalia . . . 109 9e−24 gb|ABG01139.1| disease resistance protein [Arabidopsis thaliana] 109 9e−24 gb|ABG01137.1| disease resistance protein [Arabidopsis thaliana] 109 9e−24 gb|ABG00705.1| disease resistance protein [Arabidopsis thaliana] 109 9e−24 gb|ABG01123.1| disease resistance protein [Arabidopsis thalia . . . 109 9e−24 gb|ABG00731.1| disease resistance protein [Arabidopsis thaliana] 109 9e−24 gb|ABG00703.1| disease resistance protein [Arabidopsis thaliana] 109 1e−23 gb|ABG01141.1| disease resistance protein [Arabidopsis thalia . . . 108 1e−23 gb|ABG00708.1| disease resistance protein [Arabidopsis thaliana] 108 1e−23 gb|ABG01160.1| disease resistance protein [Arabidopsis thaliana] 108 1e−23 gb|ABG01134.1| disease resistance protein [Arabidopsis thaliana] 108 2e−23 ref|NP_001068347.1| Os11g0640300 [Oryza sativa (japonica cult . . . 107 3e−23 gb|ABB00893.1| disease resistance protein [Arabidopsis thalia . . . 107 3e−23 gb|ABB00891.1| disease resistance protein [Arabidopsis thalia . . . 107 3e−23 gb|ABG01131.1| disease resistance protein [Arabidopsis thalia . . . 106 5e−23 gb|ABG00732.1| disease resistance protein [Arabidopsis thalia . . . 104 2e−22 gb|ABG01161.1| disease resistance protein [Arabidopsis thaliana] 104 2e−22 gb|ABG00707.1| disease resistance protein [Arabidopsis thaliana] 104 2e−22 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica cult . . . 104 2e−22 gb|ABG00709.1| disease resistance protein [Arabidopsis thaliana] 104 2e−22 gb|ABG00701.1| disease resistance protein [Arabidopsis thaliana] 104 3e−22 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica cult . . . 103 5e−22 gb|ABG00699.1| disease resistance protein [Arabidopsis thaliana] 103 5e−22 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica cult . . . 102 7e−22 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica cult . . . 101 2e−21 ref|NP_001055149.1| Os05g0305600 [Oryza sativa (japonica cult . . . 101 2e−21 ref|NP_001067488.1| Os11g0211300 [Oryza sativa (japonica cult . . . 101 2e−21 ref|NP_193640.1| mob1/phocein family protein [Arabidopsis tha . . . 100 4e−21 ref|NP_001068349.1| Os11g0640600 [Oryza sativa (japonica cult . . . 99.1 9e−21 gb|ABG00747.1| disease resistance protein [Arabidopsis thaliana] 97.9 2e−20 sp|O50052|DRL25_ARATH Putative disease resistance protein At4 . . . 97.5 3e−20 dbj|BAD94108.1| putative disease resistance protein [Arabidop . . . 96.4 7e−20 gb|ABG00742.1| disease resistance protein [Arabidopsis thaliana] 94.4 2e−19 emb|CAO43337.1| unnamed protein product [Vitis vinifera] 91.0 3e−18 ref|NP_001062397.1| Os08g0543000 [Oryza sativa (japonica cult . . . 89.4 7e−18 ref|NP_195056.2| ADR1-L1 (ADR1-LIKE 1); ATP binding/protein . . . 88.7 1e−17 sp|Q9SZA7|DRL29_ARATH Probable disease resistance protein At4 . . . 88.3 2e−17 emb|CAB38788.1| putative protein [Arabidopsis thaliana] >emb|. . . 88.3 2e−17 gb|ACD76094.1| VRP1-2 [Vitis hybrid cultivar] 87.5 3e−17 gb|ABG00782.1| disease resistance protein [Arabidopsis thaliana] 87.1 4e−17 gb|ABG00771.1| disease resistance protein [Arabidopsis thaliana] 86.7 4e−17 gb|ABG00813.1| disease resistance protein [Arabidopsis thaliana] 86.7 5e−17 gb|ABG00761.1| disease resistance protein [Arabidopsis thalia . . . 86.7 5e−17 gb|ABG00748.1| disease resistance protein [Arabidopsis thalia . . . 86.7 5e−17 gb|ABG00765.1| disease resistance protein [Arabidopsis thalia . . . 86.7 5e−17 gb|ABG00785.1| disease resistance protein [Arabidopsis thaliana] 86.7 5e−17 gb|ABG00770.1| disease resistance protein [Arabidopsis thaliana] 86.7 5e−17 gb|ABG00812.1| disease resistance protein [Arabidopsis thaliana] 86.7 5e−17 gb|ABG00757.1| disease resistance protein [Arabidopsis thaliana] 86.7 5e−17 gb|ABG00753.1| disease resistance protein [Arabidopsis thalia . . . 86.7 5e−17 emb|CAO70216.1| unnamed protein product [Vitis vinifera] 86.7 5e−17 gb|ABG00803.1| disease resistance protein [Arabidopsis thaliana] 86.3 6e−17 gb|ABG00804.1| disease resistance protein [Arabidopsis thaliana] 86.3 6e−17 gb|ABG00762.1| disease resistance protein [Arabidopsis thalia . . . 86.3 6e−17

APPENDIX 3 List of SNC1 homologs in species other than Arabidopsis thaliana Sequences producing significant alignments: (Bits) Value Vitis vinifera (wine grape) [eudicots] taxid 29760 emb|CAO24746.1| unnamed protein product [Vitis vinifera] 374 4e−102 emb|CAO64653.1| unnamed protein product [Vitis vinifera] 366 8e−100 emb|CAO16282.1| unnamed protein product [Vitis vinifera] 365 2e−99 emb|CAO16318.1| unnamed protein product [Vitis vinifera] 361 2e−98 emb|CAN68293.1| hypothetical protein [Vitis vinifera] 361 3e−98 emb|CAN84090.1| hypothetical protein [Vitis vinifera] 360 5e−98 emb|CAO49904.1| unnamed protein product [Vitis vinifera] 360 8e−98 emb|CAO49944.1| unnamed protein product [Vitis vinifera] 359 1e−97 emb|CAN83385.1| hypothetical protein [Vitis vinifera] 356 7e−97 emb|CAN76615.1| hypothetical protein [Vitis vinifera] 355 1e−96 emb|CAO16283.1| unnamed protein product [Vitis vinifera] 355 3e−96 emb|CAN71924.1| hypothetical protein [Vitis vinifera] 352 2e−95 emb|CAO49942.1| unnamed protein product [Vitis vinifera] 351 2e−95 emb|CAO49905.1| unnamed protein product [Vitis vinifera] 351 2e−95 emb|CAO16420.1| unnamed protein product [Vitis vinifera] 351 2e−95 emb|CAO65792.1| unnamed protein product [Vitis vinifera] 351 3e−95 emb|CAO16320.1| unnamed protein product [Vitis vinifera] 351 4e−95 emb|CAO49627.1| unnamed protein product [Vitis vinifera] 350 5e−95 emb|CAN72303.1| hypothetical protein [Vitis vinifera] 350 6e−95 emb|CAO16286.1| unnamed protein product [Vitis vinifera] 350 7e−95 emb|CAO49902.1| unnamed protein product [Vitis vinifera] 349 1e−94 emb|CAO16284.1| unnamed protein product [Vitis vinifera] 348 3e−94 emb|CAN64759.1| hypothetical protein [Vitis vinifera] 348 3e−94 emb|CAN77679.1| hypothetical protein [Vitis vinifera] 347 5e−94 emb|CAO16326.1| unnamed protein product [Vitis vinifera] 346 8e−94 emb|CAO16306.1| unnamed protein product [Vitis vinifera] 346 1e−93 emb|CAO43131.1| unnamed protein product [Vitis vinifera] 344 3e−93 emb|CAO49620.1| unnamed protein product [Vitis vinifera] 344 4e−93 emb|CAO49901.1| unnamed protein product [Vitis vinifera] 344 4e−93 emb|CAO16416.1| unnamed protein product [Vitis vinifera] 343 7e−93 emb|CAO50050.1| unnamed protein product [Vitis vinifera] 342 1e−92 emb|CAO16321.1| unnamed protein product [Vitis vinifera] 341 2e−92 emb|CAO16287.1| unnamed protein product [Vitis vinifera] 341 2e−92 emb|CAN78931.1| hypothetical protein [Vitis vinifera] 341 3e−92 emb|CAO16405.1| unnamed protein product [Vitis vinifera] 340 7e−92 emb|CAO16303.1| unnamed protein product [Vitis vinifera] 340 8e−92 emb|CAN67940.1| hypothetical protein [Vitis vinifera] 339 1e−91 emb|CAN82909.1| hypothetical protein [Vitis vinifera] 338 2e−91 emb|CAN68265.1| hypothetical protein [Vitis vinifera] 337 4e−91 emb|CAO44592.1| unnamed protein product [Vitis vinifera] 336 6e−91 emb|CAO64662.1| unnamed protein product [Vitis vinifera] 336 7e−91 emb|CAO44537.1| unnamed protein product [Vitis vinifera] 336 9e−91 emb|CAO16335.1| unnamed protein product [Vitis vinifera] 336 1e−90 emb|CAO43490.1| unnamed protein product [Vitis vinifera] 336 1e−90 emb|CAO49934.1| unnamed protein product [Vitis vinifera] 336 1e−90 emb|CAO16292.1| unnamed protein product [Vitis vinifera] 335 2e−90 emb|CAO15446.1| unnamed protein product [Vitis vinifera] 334 3e−90 emb|CAO64667.1| unnamed protein product [Vitis vinifera] 334 5e−90 emb|CAO62387.1| unnamed protein product [Vitis vinifera] 333 8e−90 emb|CAN68108.1| hypothetical protein [Vitis vinifera] 332 2e−89 emb|CAO64659.1| unnamed protein product [Vitis vinifera] 331 3e−89 emb|CAO16327.1| unnamed protein product [Vitis vinifera] 331 3e−89 emb|CAO16289.1| unnamed protein product [Vitis vinifera] 330 5e−89 emb|CAO49940.1| unnamed protein product [Vitis vinifera] 330 9e−89 emb|CAO16427.1| unnamed protein product [Vitis vinifera] 329 1e−88 emb|CAO71542.1| unnamed protein product [Vitis vinifera] 329 2e−88 emb|CAN75658.1| hypothetical protein [Vitis vinifera] 327 5e−88 emb|CAO44566.1| unnamed protein product [Vitis vinifera] 327 6e−88 emb|CAN78476.1| hypothetical protein [Vitis vinifera] 327 6e−88 emb|CAO44571.1| unnamed protein product [Vitis vinifera] 326 1e−87 emb|CAN73064.1| hypothetical protein [Vitis vinifera] 325 2e−87 emb|CAO44568.1| unnamed protein product [Vitis vinifera] 325 3e−87 emb|CAO16426.1| unnamed protein product [Vitis vinifera] 324 4e−87 emb|CAO62662.1| unnamed protein product [Vitis vinifera] 323 9e−87 emb|CAO43693.1| unnamed protein product [Vitis vinifera] 323 9e−87 emb|CAO16291.1| unnamed protein product [Vitis vinifera] 323 1e−86 emb|CAO15447.1| unnamed protein product [Vitis vinifera] 323 1e−86 emb|CAO49577.1| unnamed protein product [Vitis vinifera] 322 2e−86 emb|CAN69843.1| hypothetical protein [Vitis vinifera] 321 4e−86 emb|CAO50047.1| unnamed protein product [Vitis vinifera] 321 4e−86 emb|CAO49573.1| unnamed protein product [Vitis vinifera] 320 5e−86 emb|CAO16055.1| unnamed protein product [Vitis vinifera] 320 1e−85 emb|CAO71533.1| unnamed protein product [Vitis vinifera] 319 1e−85 emb|CAO49941.1| unnamed protein product [Vitis vinifera] 318 2e−85 emb|CAO15210.1| unnamed protein product [Vitis vinifera] 318 2e−85 emb|CAO16288.1| unnamed protein product [Vitis vinifera] 318 3e−85 emb|CAO15450.1| unnamed protein product [Vitis vinifera] 317 4e−85 emb|CAO71531.1| unnamed protein product [Vitis vinifera] 316 1e−84 emb|CAN61526.1| hypothetical protein [Vitis vinifera] 316 1e−84 emb|CAO64669.1| unnamed protein product [Vitis vinifera] 313 7e−84 emb|CAN63551.1| hypothetical protein [Vitis vinifera] 313 8e−84 emb|CAO50049.1| unnamed protein product [Vitis vinifera] 313 1e−83 emb|CAO43123.1| unnamed protein product [Vitis vinifera] 312 1e−83 emb|CAO43491.1| unnamed protein product [Vitis vinifera] 310 8e−83 emb|CAO70119.1| unnamed protein product [Vitis vinifera] 309 2e−82 emb|CAO62661.1| unnamed protein product [Vitis vinifera] 308 3e−82 emb|CAO16324.1| unnamed protein product [Vitis vinifera] 306 8e−82 emb|CAO49576.1| unnamed protein product [Vitis vinifera] 306 1e−81 emb|CAO71529.1| unnamed protein product [Vitis vinifera] 306 1e−81 emb|CAO67899.1| unnamed protein product [Vitis vinifera] 304 3e−81 emb|CAO70121.1| unnamed protein product [Vitis vinifera] 304 3e−81 emb|CAO71538.1| unnamed protein product [Vitis vinifera] 304 3e−81 emb|CAO71537.1| unnamed protein product [Vitis vinifera] 304 3e−81 emb|CAO16413.1| unnamed protein product [Vitis vinifera] 304 4e−81 emb|CAO44544.1| unnamed protein product [Vitis vinifera] 303 8e−81 emb|CAO16352.1| unnamed protein product [Vitis vinifera] 303 1e−80 emb|CAO44555.1| unnamed protein product [Vitis vinifera] 303 1e−80 emb|CAN70507.1| hypothetical protein [Vitis vinifera] 302 1e−80 emb|CAN61627.1| hypothetical protein [Vitis vinifera] 301 2e−80 emb|CAO49580.1| unnamed protein product [Vitis vinifera] 301 3e−80 emb|CAO16253.1| unnamed protein product [Vitis vinifera] 301 3e−80 emb|CAN73963.1| hypothetical protein [Vitis vinifera] 301 5e−80 emb|CAN74723.1| hypothetical protein [Vitis vinifera] 300 5e−80 emb|CAN61773.1| hypothetical protein [Vitis vinifera] 300 6e−80 emb|CAO49948.1| unnamed protein product [Vitis vinifera] 300 6e−80 emb|CAN77694.1| hypothetical protein [Vitis vinifera] 299 2e−79 emb|CAN75296.1| hypothetical protein [Vitis vinifera] 299 2e−79 emb|CAO16391.1| unnamed protein product [Vitis vinifera] 298 2e−79 emb|CAN68630.1| hypothetical protein [Vitis vinifera] 298 3e−79 emb|CAN67859.1| hypothetical protein [Vitis vinifera] 296 1e−78 emb|CAN66453.1| hypothetical protein [Vitis vinifera] 294 3e−78 emb|CAO44552.1| unnamed protein product [Vitis vinifera] 292 2e−77 emb|CAN82897.1| hypothetical protein [Vitis vinifera] 292 2e−77 emb|CAN82538.1| hypothetical protein [Vitis vinifera] 281 4e−74 emb|CAO16400.1| unnamed protein product [Vitis vinifera] 279 1e−73 emb|CAO16323.1| unnamed protein product [Vitis vinifera] 277 7e−73 emb|CAO24785.1| unnamed protein product [Vitis vinifera] 276 1e−72 emb|CAN78885.1| hypothetical protein [Vitis vinifera] 274 4e−72 emb|CAO24777.1| unnamed protein product [Vitis vinifera] 273 7e−72 emb|CAO16421.1| unnamed protein product [Vitis vinifera] 273 7e−72 emb|CAO40986.1| unnamed protein product [Vitis vinifera] 273 7e−72 emb|CAO17013.1| unnamed protein product [Vitis vinifera] 270 8e−71 emb|CAN68969.1| hypothetical protein [Vitis vinifera] 269 1e−70 emb|CAN83953.1| hypothetical protein [Vitis vinifera] 268 3e−70 emb|CAO16300.1| unnamed protein product [Vitis vinifera] 268 4e−70 emb|CAO16423.1| unnamed protein product [Vitis vinifera] 268 4e−70 emb|CAO49900.1| unnamed protein product [Vitis vinifera] 266 1e−69 emb|CAO49932.1| unnamed protein product [Vitis vinifera] 265 2e−69 emb|CAO49622.1| unnamed protein product [Vitis vinifera] 264 6e−69 emb|CAN78790.1| hypothetical protein [Vitis vinifera] 261 3e−68 emb|CAO44535.1| unnamed protein product [Vitis vinifera] 261 5e−68 emb|CAN81612.1| hypothetical protein [Vitis vinifera] 260 8e−68 emb|CAO49953.1| unnamed protein product [Vitis vinifera] 257 4e−67 emb|CAO42751.1| unnamed protein product [Vitis vinifera] 257 5e−67 emb|CAO50043.1| unnamed protein product [Vitis vinifera] 254 6e−66 emb|CAN69078.1| hypothetical protein [Vitis vinifera] 253 7e−66 emb|CAO49933.1| unnamed protein product [Vitis vinifera] 249 2e−64 emb|CAO40985.1| unnamed protein product [Vitis vinifera] 247 8e−64 emb|CAO15207.1| unnamed protein product [Vitis vinifera] 242 2e−62 emb|CAO62388.1| unnamed protein product [Vitis vinifera] 241 4e−62 emb|CAO49600.1| unnamed protein product [Vitis vinifera] 240 1e−61 emb|CAO16388.1| unnamed protein product [Vitis vinifera] 239 1e−61 emb|CAO49943.1| unnamed protein product [Vitis vinifera] 237 7e−61 emb|CAN68384.1| hypothetical protein [Vitis vinifera] 237 7e−61 emb|CAO49792.1| unnamed protein product [Vitis vinifera] 235 2e−60 emb|CAN66808.1| hypothetical protein [Vitis vinifera] 232 2e−59 emb|CAO24775.1| unnamed protein product [Vitis vinifera] 228 3e−58 emb|CAO16896.1| unnamed protein product [Vitis vinifera] 224 6e−57 emb|CAO16397.1| unnamed protein product [Vitis vinifera] 220 8e−56 emb|CAO49935.1| unnamed protein product [Vitis vinifera] 219 1e−55 emb|CAN75617.1| hypothetical protein [Vitis vinifera] 217 6e−55 emb|CAN72925.1| hypothetical protein [Vitis vinifera] 217 9e−55 emb|CAN62576.1| hypothetical protein [Vitis vinifera] 215 3e−54 emb|CAO16890.1| unnamed protein product [Vitis vinifera] 215 3e−54 emb|CAO16295.1| unnamed protein product [Vitis vinifera] 214 6e−54 emb|CAN66451.1| hypothetical protein [Vitis vinifera] 212 2e−53 emb|CAN61853.1| hypothetical protein [Vitis vinifera] 212 2e−53 emb|CAO71540.1| unnamed protein product [Vitis vinifera] 211 3e−53 emb|CAN74711.1| hypothetical protein [Vitis vinifera] 210 1e−52 emb|CAO49903.1| unnamed protein product [Vitis vinifera] 205 3e−51 emb|CAN81250.1| hypothetical protein [Vitis vinifera] 202 2e−50 emb|CAO16408.1| unnamed protein product [Vitis vinifera] 198 3e−49 emb|CAO49595.1| unnamed protein product [Vitis vinifera] 195 2e−48 emb|CAN75767.1| hypothetical protein [Vitis vinifera] 193 1e−47 emb|CAO67895.1| unnamed protein product [Vitis vinifera] 190 7e−47 emb|CAO16393.1| unnamed protein product [Vitis vinifera] 187 6e−46 emb|CAO44531.1| unnamed protein product [Vitis vinifera] 184 4e−45 emb|CAO44596.1| unnamed protein product [Vitis vinifera] 177 5e−43 emb|CAN73697.1| hypothetical protein [Vitis vinifera] 172 3e−41 emb|CAO24741.1| unnamed protein product [Vitis vinifera] 171 3e−41 emb|CAO49582.1| unnamed protein product [Vitis vinifera] 171 6e−41 emb|CAO24737.1| unnamed protein product [Vitis vinifera] 170 6e−41 emb|CAN72675.1| hypothetical protein [Vitis vinifera] 170 7e−41 emb|CAO15213.1| unnamed protein product [Vitis vinifera] 169 3e−40 emb|CAO24780.1| unnamed protein product [Vitis vinifera] 169 3e−40 emb|CAO16417.1| unnamed protein product [Vitis vinifera] 167 1e−39 emb|CAO16900.1| unnamed protein product [Vitis vinifera] 167 1e−39 emb|CAO24744.1| unnamed protein product [Vitis vinifera] 160 7e−38 emb|CAO64668.1| unnamed protein product [Vitis vinifera] 160 1e−37 emb|CAN68030.1| hypothetical protein [Vitis vinifera] 159 2e−37 emb|CAO16389.1| unnamed protein product [Vitis vinifera] 157 6e−37 emb|CAO17016.1| unnamed protein product [Vitis vinifera] 154 5e−36 emb|CAO24745.1| unnamed protein product [Vitis vinifera] 146 2e−33 emb|CAO69467.1| unnamed protein product [Vitis vinifera] 145 2e−33 emb|CAO24742.1| unnamed protein product [Vitis vinifera] 145 2e−33 emb|CAO24738.1| unnamed protein product [Vitis vinifera] 143 2e−32 emb|CAO16205.1| unnamed protein product [Vitis vinifera] 123 2e−26 emb|CAN64645.1| hypothetical protein [Vitis vinifera] 119 2e−25 emb|CAN63598.1| hypothetical protein [Vitis vinifera] 115 2e−24 emb|CAO49606.1| unnamed protein product [Vitis vinifera] 113 1e−23 emb|CAO16398.1| unnamed protein product [Vitis vinifera] 113 2e−23 emb|CAN68234.1| hypothetical protein [Vitis vinifera] 110 9e−23 emb|CAO16330.1| unnamed protein product [Vitis vinifera] 107 9e−22 emb|CAO49584.1| unnamed protein product [Vitis vinifera] 106 2e−21 emb|CAO16390.1| unnamed protein product [Vitis vinifera] 104 6e−21 emb|CAO16334.1| unnamed protein product [Vitis vinifera] 98 6e−19 emb|CAO23281.1| unnamed protein product [Vitis vinifera] 96 1e−18 emb|CAO16319.1| unnamed protein product [Vitis vinifera] 96 2e−18 emb|CAO44577.1| unnamed protein product [Vitis vinifera] 95 4e−18 emb|CAN69856.1| hypothetical protein [Vitis vinifera] 95 4e−18 emb|CAO49427.1| unnamed protein product [Vitis vinifera] 94 8e−18 emb|CAN62507.1| hypothetical protein [Vitis vinifera] 93 1e−17 emb|CAN82453.1| hypothetical protein [Vitis vinifera] 92 3e−17 emb|CAN78783.1| hypothetical protein [Vitis vinifera] 91 6e−17 emb|CAO15448.1| unnamed protein product [Vitis vinifera] 90 9e−17 emb|CAN79645.1| hypothetical protein [Vitis vinifera] 90 1e−16 emb|CAO16418.1| unnamed protein product [Vitis vinifera] 90 1e−16 gb|AAQ15191.1|AF365879_1 resistance protein [Vitis vinifera] 89 2e−16 emb|CAO49611.1| unnamed protein product [Vitis vinifera] 88 4e−16 emb|CAO44569.1| unnamed protein product [Vitis vinifera] 88 5e−16 emb|CAO66485.1| unnamed protein product [Vitis vinifera] 88 5e−16 emb|CAO44573.1| unnamed protein product [Vitis vinifera] 88 5e−16 emb|CAO44572.1| unnamed protein product [Vitis vinifera] 88 5e−16 emb|CAN64358.1| hypothetical protein [Vitis vinifera] 87 8e−16 emb|CAO61278.1| unnamed protein product [Vitis vinifera] 86 1e−15 emb|CAN63745.1| hypothetical protein [Vitis vinifera] 85 4e−15 emb|CAO50045.1| unnamed protein product [Vitis vinifera] 83 1e−14 emb|CAO49575.1| unnamed protein product [Vitis vinifera] 83 2e−14 emb|CAO14504.1| unnamed protein product [Vitis vinifera] 78 3e−13 emb|CAN76072.1| hypothetical protein [Vitis vinifera] 78 4e−13 Populus trichocarpa (black cottonwood, . . . ) [eudicots] taxid 3694 gb|ABF81417.1| TIR-NBS-LRR type disease resistance protein . . . 346 1e−93 gb|ABF81413.1| TIR-NBS-LRR type disease resistance protein . . . 344 5e−93 gb|ABF81439.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 342 1e−92 gb|ABF81428.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 340 4e−92 gb|ABF81437.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 339 1e−91 gb|ABF81434.1| TIR-NBS-TIR type disease resistance protein . . . 339 1e−91 gb|ABF81431.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 338 2e−91 gb|ABF81454.1| TIR-NBS-LRR type disease resistance protein . . . 338 2e−91 gb|ABF81431.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 63 2e−08 gb|ABF81454.1| TIR-NBS-LRR type disease resistance protein . . . 63 2e−08 gb|ABF81431.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 39 0.27 gb|ABF81454.1| TIR-NBS-LRR type disease resistance protein . . . 39 0.27 gb|ABF81414.1| TIR-NBS-LRR type disease resistance protein . . . 338 2e−91 gb|ABF81427.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 338 3e−91 gb|ABF81441.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 337 4e−91 gb|ABF81445.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 337 4e−91 gb|ABF81441.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 65 4e−09 gb|ABF81445.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 65 4e−09 gb|ABF81441.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 65 5e−09 gb|ABF81445.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 65 5e−09 gb|ABF81438.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 336 8e−91 gb|ABF81430.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 336 1e−90 gb|ABG37662.1| NBS-LRR type disease resistance-like protei . . . 334 4e−90 gb|ABF81423.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 334 4e−90 gb|ABF81459.1| TIR-NBS type disease resistance protein [Po . . . 333 7e−90 gb|ABF81416.1| NBS-LRR-TIR type disease resistance protein . . . 330 5e−89 gb|ABB82027.1| TIR-NBS disease resistance-like protein [Po . . . 330 9e−89 gb|ABF81433.1| TIR-NBS-TIR type disease resistance protein . . . 329 1e−88 gb|ABF81409.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 327 6e−88 gb|ABF81410.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 327 6e−88 gb|ABF81409.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 193 9e−48 gb|ABF81410.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 193 9e−48 gb|ABF81409.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 76 1e−12 gb|ABF81410.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 76 1e−12 gb|ABF81409.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 68 5e−10 gb|ABF81410.1| TIR-NBS-NBS-LRR type disease resistance pro . . . 68 5e−10 gb|ABB82031.1| TIR-NBS disease resistance-like protein [Po . . . 324 3e−87 gb|ABB82024.1| TIR-NBS disease resistance-like protein [Po . . . 321 2e−86 gb|ABB82028.1| TIR-NBS disease resistance-like protein [Po . . . 321 4e−86 gb|ABE99702.1| TIR-NBS-LRR disease resistance-like protein . . . 314 3e−84 gb|ABB82029.1| TIR-NBS disease resistance-like protein [Po . . . 314 4e−84 gb|ABF81419.1| TIR-NBS-LRR type disease resistance protein . . . 300 6e−80 gb|ABF81418.1| NBS type disease resistance protein [Populu . . . 297 5e−79 gb|ABF81429.1| TIR-NBS-TIR type disease resistance protein . . . 287 5e−76 gb|ABB82026.1| TIR-NBS disease resistance-like protein [Po . . . 281 3e−74 gb|ABF81471.1| TIR-NBS type disease resistance protein [Po . . . 275 2e−72 gb|ABF81452.1| TIR-NBS type disease resistance protein [Po . . . 264 4e−69 gb|ABB82025.1| TIR-NBS disease resistance-like protein [Po . . . 250 9e−65 gb|ABF81440.1| TIR-NBS-LRR-TIR type disease resistance pro . . . 243 7e−63 gb|ABB82030.1| TIR-NBS disease resistance-like protein [Po . . . 242 2e−62 gb|ABF81412.1| NBS type disease resistance protein [Populu . . . 198 4e−49 gb|ABF81465.1| TIR-NBS-LRR type disease resistance protein . . . 145 3e−33 gb|ABF81432.1| TIR-NBS-TIR-TIR-WRKY type disease resistanc . . . 137 1e−30 gb|ABF81408.1| NBS type disease resistance protein [Populu . . . 103 2e−20 Solanum tuberosum (potatoes) [eudicots] taxid 4113 gb|AAP44393.1| nematode resistance-like protein [Solanum t . . . 324 3e−87 gb|AAP44392.1| nematode resistance-like protein [Solanum t . . . 323 7e−87 gb|AAP44394.1| nematode resistance-like protein [Solanum t . . . 322 2e−86 gb|AAP44390.1| nematode resistance protein [Solanum tubero . . . 321 2e−86 gb|AAP44391.1| nematode resistance-like protein [Solanum t . . . 314 5e−84 emb|CAA08798.1| NL27 [Solanum tuberosum] 304 4e−81 Cucumis melo (Oriental melon) [eudicots] taxid 3656 gb|AAU04762.1| MRGH21 [Cucumis melo] 321 2e−86 gb|AAU04761.1| MRGH13 [Cucumis melo] 317 4e−85 gb|AAU04763.1| MRGH8 [Cucumis melo] 305 2e−81 gb|ABB91439.1| MRGH-J [Cucumis melo] 288 3e−76 gb|AAU04760.1| MRGH12 [Cucumis melo] 287 5e−76 gb|AAO45748.1| MRGH5 [Cucumis melo] 262 1e−68 gb|ABR67409.1| melon resistance protein-like protein [Cucu . . . 262 2e−68 gb|AAU04759.1| MRGH11 [Cucumis melo] 262 2e−68 gb|AAO45749.1| MRGH63 [Cucumis melo] 235 3e−60 gb|AAU04764.1| MRGH9 [Cucumis melo] 233 9e−60 gb|AAU04758.1| MRGH10 [Cucumis melo] 183 1e−44 Medicago sativa (alfalfa, . . . ) [eudicots] taxid 3879 gb|ACF19651.1| TIR-NBS-LRR RCT1-like resistance protein [M . . . 321 4e−86 Populus balsamifera (balsam poplar, . . . ) [eudicots] taxid 73824 gb|ABE99701.1| TIR-NBS-LRR disease resistance-like protein . . . 317 4e−85 Phaseolus vulgaris (French bean, . . . ) [eudicots] taxid 3885 gb|ABH07384.1| CMR1 [Phaseolus vulgaris] 309 2e−82 gb|ABA00702.1| disease resistance protein [Phaseolus vulga . . . 171 4e−41 Glycine max (soybeans) [eudicots] taxid 3847 gb|AAO23067.1| R 12 protein [Glycine max] 306 8e−82 gb|AAO23066.1| R 3 protein [Glycine max] 305 2e−81 gb|AAO23077.1| R 8 protein [Glycine max] 304 4e−81 gb|AAO23075.1| R 5 protein [Glycine max] 304 4e−81 gb|AAO23069.1| R 4 protein [Glycine max] 303 1e−80 gb|AAO92748.1| candidate disease-resistance protein SR1 [G . . . 302 1e−80 gb|AAO23074.1| R 10 protein [Glycine max] 298 3e−79 gb|AAO23076.1| R 1 protein [Glycine max] 298 3e−79 gb|AAL56987.1| AF327903_1 functional candidate resistance p . . . 289 1e−76 gb|AAG48132.1| AF322632_1 putative resistance protein [Glyc . . . 284 3e−75 gb|AAG09951.1| resistance protein LM6 [Glycine max] 282 2e−74 gb|AAG09953.1| AF175398_1 resistance protein MG63 [Glycine . . . 178 4e−43 gb|AAN63807.1| resistance protein KR3 [Glycine max] 166 1e−39 gb|AAL57179.1| AF345652_1 functional resistance protein KR2 . . . 162 2e−38 gb|AAP74724.1| disease resistance-like protein KR7 [Glycin . . . 161 4e−38 gb|AAP74723.1| disease resistance-like protein KR6 [Glycin . . . 160 8e−38 gb|AAP74722.1| disease resistance-like protein KR5 [Glycin . . . 158 3e−37 gb|AAG09952.1| AF175389_1 resistance protein LM17 [Glycine . . . 153 8e−36 gb|AAM90028.1| AF403282_1 disease resistance-like protein G . . . 142 2e−32 gb|AMG01048.1| resistance protein LM17.2 [Glycine max] 142 2e−32 gb|AAM90026.1| AF403280_1 disease resistance-like protein G . . . 142 3e−32 gb|AAM90025.1| AF403279_1 disease resistance-like protein G . . . 142 3e−32 gb|AAM90024.1| AF403278_1 disease resistance-like protein G . . . 140 8e−32 gb|AAM90027.1| AF403281_1 disease resistance-like protein G . . . 140 1e−31 gb|AAM90029.1| AF403283_1 disease resistance-like protein G . . . 125 4e−27 gb|AAM90030.1| AF403284_1 disease resistance-like protein G . . . 123 1e−26 gb|AAM90031.1| AF403285_1 disease resistance-like protein G . . . 123 2e−26 emb|CAA06201.1| resistance protein [Glycine max] 106 2e−21 gb|AAG48133.1| AF322633_1 putative resistance protein [Glyc . . . 102 2e−20 gb|AAM90014.1| AF403267_1 disease resistance-like protein G . . . 98 3e−19 gb|AAM90010.1| AF403263_1 disease resistance-like protein G . . . 98 3e−19 gb|AAM90013.1| AF403266_1 disease resistance-like protein G . . . 98 3e−19 gb|AAM90012.1| AF403265_1 disease resistance-like protein G . . . 98 4e−19 gb|AAM90008.1| AF403261_1 disease resistance-like protein G . . . 97 7e−19 gb|AAM90009.1| AF403262_1 disease resistance-like protein G . . . 97 1e−18 gb|AAM90022.1| AF403276_1 disease resistance-like protein G . . . 95 5e−18 gb|AAM90011.1| AF403264_1 disease resistance-like protein G . . . 94 8e−18 gb|AAM90023.1| AF403277_1 disease resistance-like protein G . . . 93 1e−17 gb|AAM90017.1| AF403271_1 disease resistance-like protein G . . . 93 1e−17 gb|AAM90018.1| AF403272_1 disease resistance-like protein G . . . 92 2e−17 gb|AAM90021.1| AF403275_1 disease resistance-like protein G . . . 92 3e−17 gb|AAM90020.1| AF403274_1 disease resistance-like protein G . . . 91 4e−17 gb|AAM90019.1| AF403273_1 disease resistance-like protein G . . . 88 4e−16 Medicago truncatula [eudicots] taxid 3880 gb|ACF19650.1| TIR-NBS-LRR RCT1 resistance protein [Medica . . . 304 3e−81 gb|ABD28507.1| Leucine-rich repeat; Leucine-rich [Medicago . . . 301 4e−80 gb|ABN05946.1| TIR [Medicago truncatula] 300 6e−80 gb|ABD33309.1| Ribonuclease H [Medicago truncatula] 299 1e−79 gb|ABD33387.2| TIR [Medicago truncatula] 298 2e−79 gb|ABD28703.1| TIR [Medicago truncatula] 294 3e−78 gb|ABN09183.1| TIR; AAA ATPase [Medicago truncatula] 283 9e−75 gb|ABN09142.1| TIR [Medicago truncatula] 252 1e−65 gb|ABN08493.1| Leucine-rich repeat, typical subtype [Medic . . . 103 1e−20 Nicotiana tabacum (tobacco, . . . ) [eudicots] taxid 4097 gb|AAT37497.1| N-like protein [Nicotiana tabacum] 295 2e−78 dbj|BAF95889.1| N-like protein [Nicotiana tabacum] 289 1e−76 dbj|BAF95888.1| N-like protein [Nicotiana tabacum] 279 2e−73 gb|ABO21407.1| TMV resistance protein N [Nicotiana tabacum] 278 2e−73 dbj|BAD12594.1| N protein [Nicotiana tabacum] 278 3e−73 dbj|BAD12595.1| truncated N protein [Nicotiana tabacum] 175 4e−42 gb|AAG43546.1| AF211528_1 Avr9/Cf-9 rapidly elicited protei . . . 95 3e−18 Malus baccata (shan jing zi) [eudicots] taxid 106549 gb|AAQ93075.1| TIR-NBS-LRR type R protein 7 [Malus baccata] 289 9e−77 gb|AAQ93074.1| putative TIR-NBS type R protein 4 [Malus ba . . . 178 4e−43 gb|AAQ93076.1| putative TIR-NBS type R protein 4 [Malus ba . . . 178 4e−43 Populus deltoides [eudicots] taxid 3696 emb|CAC95124.1| TIR/NBS/LRR protein [Populus deltoides] 281 5e−74 Nicotiana glutinosa [eudicots] taxid 35889 sp|Q40392|TMVRN_NICGU TMV resistance protein N 278 3e−73 gb|AAA50763.1| N 278 3e−73 sp|Q40392|TMVRN_NICGU TMV resistance protein N 59 3e−07 gb|AAA50763.1| N 59 3e−07 sp|Q40392|TMVRN_NICGU TMV resistance protein N 47 8e−04 gb|AAA50763.1| N 47 8e−04 sp|Q40392|TMVRN_NICGU TMV resistance protein N 41 0.054 gb|AAA50763.1| N 41 0.054 Solanum lycopersicum (tomato) [eudicots] taxid 4081 gb|AAR21295.1| bacterial spot disease resistance protein 4 . . . 273 8e−72 Solanum tuberosum subsp. andigena [eudicots] taxid 80418 emb|CAC82811.1| resistance gene-like [Solanum tuberosum su . . . 265 2e−69 emb|CAC82812.1| resistance gene-like [Solanum tuberosum su . . . 265 3e−69 Lens culinaris [eudicots] taxid 3864 emb|CAD56833.1| putative resistance gene analogue protein . . . 264 5e−69 Arabidopsis lyrata (lyrate rockcress) [eudicots] taxid 59689 gb|ABB00841.1| disease resistance protein [Arabidopsis lyr . . . 251 5e−65 gb|ABF74395.1| disease resistance protein [Arabidopsis lyr . . . 148 3e−34 gb|ABF74396.1| disease resistance protein [Arabidopsis lyr . . . 139 2e−31 gb|ABF74397.1| disease resistance protein [Arabidopsis lyr . . . 126 2e−27 gb|ABB00900.1| disease resistance protein [Arabidopsis lyr . . . 100 1e−19 Helianthus annuus [eudicots] taxid 4232 gb|AAN73007.1| NBS-LRR resistance protein RS6-8 [Helianthu . . . 246 1e−63 gb|AAL07535.1| resistance gene analog PU3 [Helianthus annuus] 218 4e−55 gb|AAN73009.1| NBS-LRR resistance protein RS7-4 [Helianthu . . . 139 2e−31 Linum usitatissimum [eudicots] taxid 4006 gb|AAK28809.1| AF310962_1 resistance-like protein P3-B [Lin . . . 219 2e−55 gb|AAK28812.1| AF310968_1 resistance-like protein PH-B [Lin . . . 213 9e−54 gb|AAK28806.1| AF310960_2 P2 rust resistance protein [Linum . . . 203 1e−50 gb|AAK28803.1| AF310958_1 resistance-like protein P1-A [Lin . . . 202 2e−50 gb|AAK28810.1| AF310964_1 resistance-like protein P4-B [Lin . . . 200 7e−50 gb|AAK28811.1| AF310966_1 resistance-like protein P-B [Linu . . . 200 8e−50 gb|AAK28805.1| AF310960_1 resistance-like protein P2-A [Lin . . . 196 1e−48 gb|AAK28808.1| AF310961_1 resistance-like protein P3-A [Lin . . . 194 5e−48 gb|AAK28804.1| AF310959_1 resistance-like protein P1-B [Lin . . . 186 1e−45 emb|CAC35326.1| Ngc-C protein [Linum usitatissimum] 158 4e−37 emb|CAC35339.1| Nho-C protein [Linum usitatissimum] 158 4e−37 emb|CAC35321.1| Ngc-D protein [Linum usitatissimum] 157 6e−37 emb|CAC35337.1| Nbi-C protein [Linum usitatissimum] 157 9e−37 emb|CAC35329.1| N1-C protein [Linum usitatissimum] 156 2e−36 emb|CAC35338.1| Nbi-D protein [Linum usitatissimum] 152 2e−35 emb|CAC35334.1| N2-D protein [Linum usitatissimum] 152 2e−35 emb|CAC35327.1| N1-A protein [Linum usitatissimum] 152 3e−35 emb|CAC35333.1| N2-C protein [Linum usitatissimum] 152 3e−35 emb|CAC35330.1| N1-D protein [Linum usitatissimum] 150 8e−35 emb|CAC35325.1| Ngc-B protein [Linum usitatissimum] 146 1e−33 emb|CAC35336.1| Nbi-B protein [Linum usitatissimum] 146 1e−33 emb|CAC35325.1| Ngc-B protein [Linum usitatissimum] 66 2e−09 emb|CAC35336.1| Nbi-B protein [Linum usitatissimum] 66 2e−09 emb|CAC35325.1| Ngc-B protein [Linum usitatissimum] 58 6e−07 emb|CAC35336.1| Nbi-B protein [Linum usitatissimum] 58 6e−07 emb|CAC35325.1| Ngc-B protein [Linum usitatissimum] 54 8e−06 emb|CAC35336.1| Nbi-B protein [Linum usitatissimum] 54 8e−06 emb|CAC35332.1| N2-B protein [Linum usitatissimum] 145 4e−33 emb|CAC35328.1| N1-B protein [Linum usitatissimum] 144 7e−33 emb|CAC35331.1| N2-A protein [Linum usitatissimum] 143 1e−32 emb|CAC35323.1| Ngc-A protein [Linum usitatissimum] 143 1e−32 gb|AAB47618.1| rust resistance protein M [Linum usitatissi . . . 134 7e−30 gb|AAD25974.1| AF093647_1 flax rust resistance protein [Lin . . . 123 2e−26 gb|AAD25975.1| AF093648_2 flax rust resistance protein [Lin . . . 122 2e−26 gb|AAD25976.1| AF093649_1 flax rust resistance protein [Lin . . . 120 9e−26 gb|AAD25971.1| AF093644_1 flax rust resistance protein [Lin . . . 120 1e−25 gb|AAD25967.1| AF093640_1 flax rust resistance protein [Lin . . . 120 1e−25 gb|AAD25970.1| AF093643_1 flax rust resistance protein [Lin . . . 120 1e−25 gb|AAD25967.1| AF093640_1 flax rust resistance protein [Lin . . . 57 9e−07 gb|AAD25970.1| AF093643_1 flax rust resistance protein [Lin . . . 57 9e−07 gb|AAD25967.1| AF093640_1 flax rust resistance protein [Lin . . . 46 0.002 gb|AAD25970.1| AF093643_1 flax rust resistance protein [Lin . . . 46 0.002 gb|AAD25967.1| AF093640_1 flax rust resistance protein [Lin . . . 45 0.003 gb|AAD25970.1| AF093643_1 flax rust resistance protein [Lin . . . 45 0.003 gb|AAD25967.1| AF093640_1 flax rust resistance protein [Lin . . . 35 3.4 gb|AAD25970.1| AF093643_1 flax rust resistance protein [Lin . . . 35 3.4 gb|AAD25965.1| AF093638_1 flax rust resistance protein [Lin . . . 118 3e−25 gb|AAD25972.1| AF093645_1 flax rust resistance protein [Lin . . . 117 6e−25 gb|AAD25966.1| AF093639_1 flax rust resistance protein [Lin . . . 116 2e−24 gb|AAD25969.1| AF093642_1 flax rust resistance protein [Lin . . . 115 4e−24 gb|AAD25968.1| AF093641_2 flax rust resistance protein [Lin . . . 105 4e−21 gb|AAD25973.1| AF093646_1 flax rust resistance protein [Lin . . . 102 3e−20 gb|AAA91022.1| L6 102 3e−20 gb|AAA91021.1| L6tr 101 4e−20 (Populus tomentosa × P. bolleana) × P. tomentosa var. truncata [eudicots] taxid 328805 gb|ABC55465.1| TIR-NBS disease resistance-like protein [(P . . . 208 4e−52 gb|ABC55466.1| TIR-NBS disease resistance-like protein [(P . . . 208 4e−52 Pinus taeda [conifers] taxid 3352 gb|AAM28909.1| NBS/LRR [Pinus taeda] 205 3e−51 gb|AAM28911.1| NBS/LRR [Pinus taeda] 109 2e−22 gb|AAM28912.1| NBS/LRR [Pinus taeda] 103 1e−20 gb|AAM28915.1| NBS [Pinus taeda] 101 3e−20 gb|AAM28917.1| putative TIR/NBS/LRR disease resistance pro . . . 96 1e−18 (Populus tomentosa × P. bolleana) × P. tomentosa [eudicots] taxid 418444 gb|ABM55687.1| TIR-NBS-LRR class disease resistance protei . . . 201 5e−50 Solanum demissum [eudicots] taxid 50514 gb|AAW28561.2| TMV resistance protein N, putative [Solanum . . . 172 2e−41 gb|ABI34382.1| Disease resistance protein, putative [Solan . . . 122 2e−26 gb|ABI34381.1| Leucine Rich Repeat family protein [Solanu . . . 110 1e−22 Oryza sativa Indica Group (Indian rice) [monocots] taxid 39946 gb|EAY77148.1| hypothetical protein OsI_004995 [Oryza sati . . . 121 6e−26 gb|EAY84492.1| hypothetical protein OsI_005725 [Oryza sati . . . 109 2e−22 gb|EAZ08637.1| hypothetical protein OsI_029869 [Oryza sati . . . 95 3e−18 gb|EAY73380.1| hypothetical protein OsI_001227 [Oryza sati . . . 94 6e−18 gb|EAY77149.1| hypothetical protein OsI_004996 [Oryza sati . . . 94 7e−18 gb|EAZ06275.1| hypothetical protein OsI_027507 [Oryza sati . . . 92 3e−17 gb|EAZ08636.1| hypothetical protein OsI_029868 [Oryza sati . . . 91 4e−17 gb|EAZ03476.1| hypothetical protein OsI_024708 [Oryza sati . . . 89 2e−16 gb|EAY73511.1| hypothetical protein OsI_001358 [Oryza sati . . . 89 2e−16 gb|EAY80338.1| hypothetical protein OsI_034297 [Oryza sati . . . 88 4e−16 gb|EAY80341.1| hypothetical protein OsI_034300 [Oryza sati . . . 85 4e−15 emb|CAH67345.1| OSIGBa0130B08.5 [Oryza sativa (indica cult . . . 84 5e−15 gb|EAY94648.1| hypothetical protein OsI_015881 [Oryza sati . . . 84 5e−15 emb|CAH67345.1| OSIGBa0130B08.5 [Oryza sativa (indica cult . . . 62 4e−08 gb|EAY94648.1| hypothetical protein OsI_015881 [Oryza sati . . . 62 4e−08 emb|CAH67345.1| OSIGBa0130B08.5 [Oryza sativa (indica cult . . . 46 0.002 gb|EAY94648.1| hypothetical protein OsI_015881 [Oryza sati . . . 46 0.002 emb|CAH67345.1| OSIGBa0130B08.5 [Oryza sativa (indica cult . . . 41 0.085 gb|EAY94648.1| hypothetical protein OsI_015881 [Oryza sati . . . 41 0.085 gb|EAY80353.1| hypothetical protein OsI_034312 [Oryza sati . . . 83 1e−14 Oryza sativa Japonica Group (Japanese rice) [monocots] taxid 39947 gb|EAZ14770.1| hypothetical protein OsJ_004595 [Oryza sati . . . 119 2e−25 ref|NP_001045334.1| Os01g0937300 [Oryza sativa (japonica c . . . 115 2e−24 dbj|BAF07248.1| Os01g0937300 [Oryza sativa (japonica culti . . . 115 2e−24 ref|NP_001045334.1| Os01g0937300 [Oryza sativa (japonica c . . . 98 4e−19 dbj|BAF07248.1| Os01g0937300 [Oryza sativa (japonica culti . . . 98 4e−19 ref|NP_001045334.1| Os01g0937300 [Oryza sativa (japonica c . . . 79 2e−13 dbj|BAF07248.1| Os01g0937300 [Oryza sativa (japonica culti . . . 79 2e−13 dbj|BAD87306.1| putative blight resistance protein [Oryza . . . 114 8e−24 gb|EAZ21756.1| hypothetical protein OsJ_005239 [Oryza sati . . . 109 2e−22 dbj|BAD38047.1| putative NBS-LRR resistance protein RGH2 [. . . 105 5e−21 ref|NP_001062892.1| Os09g0327800 [Oryza sativa (japonica c . . . 96 2e−18 dbj|BAF24806.1| Os09g0327800 [Oryza sativa (japonica culti . . . 96 2e−18 ref|NP_001062892.1| Os09g0327800 [Oryza sativa (japonica c . . . 58 5e−07 dbj|BAF24806.1| Os09g0327800 [Oryza sativa (japonica culti . . . 58 5e−07 gb|EAZ44276.1| hypothetical protein OsJ_027759 [Oryza sati . . . 95 2e−18 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 95 4e−18 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 95 4e−18 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 95 4e−18 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 95 4e−18 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 85 3e−15 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 85 3e−15 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 85 3e−15 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 85 3e−15 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 76 2e−12 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 76 2e−12 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 76 2e−12 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 76 2e−12 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 67 7e−10 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 67 7e−10 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 67 7e−10 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 67 7e−10 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 59 2e−07 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 59 2e−07 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 59 2e−07 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 59 2e−07 ref|NP_001042644.1| Os01g0260500 [Oryza sativa (japonica c . . . 59 2e−07 dbj|BAB03441.1| NBS-LRR disease resistance protein-like [. . . 59 2e−07 dbj|BAF04558.1| Os01g0260500 [Oryza sativa (japonica culti . . . 59 2e−07 gb|EAZ11314.1| hypothetical protein OsJ_001139 [Oryza sati . . . 59 2e−07 gb|EAZ14771.1| hypothetical protein OsJ_004596 [Oryza sati . . . 93 2e−17 gb|EAZ42101.1| hypothetical protein OsJ_025584 [Oryza sati . . . 92 3e−17 gb|EAZ44275.1| hypothetical protein OsJ_027758 [Oryza sati . . . 91 4e−17 dbj|BAD23605.1| NBS-LRR disease resistance protein-like [O . . . 91 4e−17 dbj|BAD23621.1| blight resistance protein SH20-like [Oryza . . . 91 4e−17 gb|EAZ44283.1| hypothetical protein OsJ_027766 [Oryza sati . . . 91 4e−17 dbj|BAD23621.1| blight resistance protein SH20-like [Oryza . . . 67 7e−10 gb|EAZ44283.1| hypothetical protein OsJ_027766 [Oryza sati . . . 67 7e−10 dbj|BAC84623.1| putative disease resistance protein [Oryza . . . 90 1e−16 dbj|BAD31615.1| putative disease resistance protein [Oryza . . . 90 1e−16 dbj|BAC84623.1| putative disease resistance protein [Oryza . . . 83 2e−14 dbj|BAD31615.1| putative disease resistance protein [Oryza . . . 83 2e−14 dbj|BAC84623.1| putative disease resistance protein [Oryza . . . 58 5e−07 dbj|BAD31615.1| putative disease resistance protein [Oryza . . . 58 5e−07 dbj|BAC84623.1| putative disease resistance protein [Oryza . . . 56 2e−06 dbj|BAD31615.1| putative disease resistance protein [Oryza . . . 56 2e−06 dbj|BAC84623.1| putative disease resistance protein [Oryza . . . 35 3.1 dbj|BAD31615.1| putative disease resistance protein [Oryza . . . 35 3.1 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 90 2e−16 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 90 2e−16 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 82 3e−14 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 82 3e−14 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 58 7e−07 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 58 7e−07 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 56 2e−06 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 56 2e−06 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 38 0.35 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 38 0.35 ref|NP_001059355.1| Os07g0273700 [Oryza sativa (japonica c . . . 35 4.2 dbj|BAF21269.1| Os07g0273700 [Oryza sativa (japonica culti . . . 35 4.2 gb|EAZ39387.1| hypothetical protein OsJ_022870 [Oryza sati . . . 89 2e−16 dbj|BAD37434.1| putative NBS-LRR disease resistance protei . . . 88 4e−16 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 86 2e−15 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 86 2e−15 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 86 2e−15 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 86 2e−15 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 70 1e−10 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 70 1e−10 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 70 1e−10 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 70 1e−10 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 70 1e−10 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 70 1e−10 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 70 1e−10 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 70 1e−10 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 60 9e−08 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 60 9e−08 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 60 9e−08 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 60 9e−08 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 59 2e−07 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 59 2e−07 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 59 2e−07 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 59 2e−07 ref|NP_001067491.1| Os11g0212000 [Oryza sativa (japonica c . . . 35 3.3 gb|ABA92120.1| Leucine Rich Repeat family protein, express . . . 35 3.3 dbj|BAF27854.1| Os11g0212000 [Oryza sativa (japonica culti . . . 35 3.3 gb|EAZ17800.1| hypothetical protein OsJ_032009 [Oryza sati . . . 35 3.3 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica c . . . 86 2e−15 dbj|BAF20099.1| Os06g0644300 [Oryza sativa (japonica culti . . . 86 2e−15 gb|EAZ37801.1| hypothetical protein OsJ_021284 [Oryza sati . . . 86 2e−15 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica c . . . 83 2e−14 dbj|BAF20099.1| Os06g0644300 [Oryza sativa (japonica culti . . . 83 2e−14 gb|EAZ37801.1| hypothetical protein OsJ_021284 [Oryza sati . . . 83 2e−14 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica c . . . 82 3e−14 dbj|BAF20099.1| Os06g0644300 [Oryza sativa (japonica culti . . . 82 3e−14 gb|EAZ37801.1| hypothetical protein OsJ_021284 [Oryza sati . . . 82 3e−14 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica c . . . 50 1e−04 dbj|BAF20099.1| Os06g0644300 [Oryza sativa (japonica culti . . . 50 1e−04 gb|EAZ37801.1| hypothetical protein OsJ_021284 [Oryza sati . . . 50 1e−04 ref|NP_001058185.1| Os06g0644300 [Oryza sativa (japonica c . . . 34 6.0 dbj|BAF20099.1| Os06g0644300 [Oryza sativa (japonica culti . . . 34 6.0 gb|EAZ37801.1| hypothetical protein OsJ_021284 [Oryza sati . . . 34 6.0 ref|NP_001067488.1| Os11g0211300 [Oryza sativa (japonica c . . . 85 3e−15 gb|ABA92038.1| Leucine Rich Repeat family protein, express . . . 85 3e−15 dbj|BAF27851.1| Os11g0211300 [Oryza sativa (japonica culti . . . 85 3e−15 ref|NP_001067488.1| Os11g0211300 [Oryza sativa (japonica c . . . 80 9e−14 gb|ABA92038.1| Leucine Rich Repeat family protein, express . . . 80 9e−14 dbj|BAF27851.1| Os11g0211300 [Oryza sativa (japonica culti . . . 80 9e−14 ref|NP_001067488.1| Os11g0211300 [Oryza sativa (japonica c . . . 59 2e−07 gb|ABA92038.1| Leucine Rich Repeat family protein, express . . . 59 2e−07 dbj|BAF27851.1| Os11g0211300 [Oryza sativa (japonica culti . . . 59 2e−07 ref|NP_001067488.1| Os11g0211300 [Oryza sativa (japonica c . . . 54 5e−06 gb|ABA92038.1| Leucine Rich Repeat family protein, express . . . 54 5e−06 dbj|BAF27851.1| Os11g0211300 [Oryza sativa (japonica culti . . . 54 5e−06 emb|CAE02491.1| OSJNBa0076N16.14 [Oryza sativa (japonica c . . . 85 5e−15 emb|CAE01665.2| OSJNBa0084K20.16 [Oryza sativa (japonica c . . . 85 5e−15 emb|CAE02491.1| OSJNBa0076N16.14 [Oryza sativa (japonica c . . . 62 3e−08 emb|CAE01665.2| OSJNBa0084K20.16 [Oryza sativa (japonica c . . . 62 3e−08 emb|CAE02491.1| OSJNBa0076N16.14 [Oryza sativa (japonica c . . . 46 0.002 emb|CAE01665.2| OSJNBa0084K20.16 [Oryza sativa (japonica c . . . 46 0.002 emb|CAE02491.1| OSJNBa0076N16.14 [Oryza sativa (japonica c . . . 41 0.085 emb|CAE01665.2| OSJNBa0084K20.16 [Oryza sativa (japonica c . . . 41 0.085 gb|EAZ31189.1| hypothetical protein OsJ_014672 [Oryza sati . . . 84 7e−15 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 83 1e−14 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 83 1e−14 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 83 1e−14 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 78 5e−13 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 78 5e−13 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 78 5e−13 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 65 5e−09 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 65 5e−09 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 65 5e−09 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 57 9e−07 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 57 9e−07 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 57 9e−07 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 53 2e−05 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 53 2e−05 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 53 2e−05 ref|NP_001067497.1| Os11g0213700 [Oryza sativa (japonica c . . . 48 4e−04 dbj|BAF27860.1| Os11g0213700 [Oryza sativa (japonica culti . . . 48 4e−04 gb|EAZ17813.1| hypothetical protein OsJ_032022 [Oryza sati . . . 48 4e−04 gb|ABA92135.1| Leucine Rich Repeat family protein, express . . . 82 2e−14 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica c . . . 81 4e−14 dbj|BAD21628.1| L-zip + NBS + LRR-like protein [Oryza sativa J . . . 81 4e−14 dbj|BAF09240.1| Os02g0597300 [Oryza sativa (japonica culti . . . 81 4e−14 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica c . . . 81 7e−14 dbj|BAD21628.1| L-zip + NBS + LRR-like protein [Oryza sativa J . . . 81 7e−14 dbj|BAF09240.1| Os02g0597300 [Oryza sativa (japonica culti . . . 81 7e−14 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica c . . . 76 2e−12 dbj|BAD21628.1| L-zip + NBS + LRR-like protein [Oryza sativa J . . . 76 2e−12 dbj|BAF09240.1| Os02g0597300 [Oryza sativa (japonica culti . . . 76 2e−12 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica c . . . 48 6e−04 dbj|BAD21628.1| L-zip + NBS + LRR-like protein [Oryza sativa J . . . 48 6e−04 dbj|BAF09240.1| Os02g0597300 [Oryza sativa (japonica culti . . . 48 6e−04 ref|NP_001047326.1| Os02g0597300 [Oryza sativa (japonica c . . . 47 0.001 dbj|BAD21628.1| L-zip + NBS + LRR-like protein [Oryza sativa J . . . 47 0.001 dbj|BAF09240.1| Os02g0597300 [Oryza sativa (japonica culti . . . 47 0.001 Picea sitchensis [conifers] taxid 3332 gb|ABK24822.1| unknown [Picea sitchensis] 115 3e−24 Hordeum vulgare (barley) [monocots] taxid 4513 emb|CAD45029.1| NBS-LRR disease resistance protein homolog . . . 115 5e−24

APPENDIX 4 Potential R mutations that could confer heat-stable disease resistance Arabidopsis thaliana >ref|NP_849398.1| RPP5 (RECOGNITION OF PERONOSPORA PARASITICA 5) E646K >ref|NP_190034.2| RPP1 (RECOGNITION OF PERONOSPORA PARASITICA 1) E741K K743D >ref|NP_199338.1| RPS4 (RESISTANT TO P. SYRINGAE 4) N689D or E801K I803D Populus trichocarpa (black cottonwood) >gb|ABF81417.1| TIR-NBS-LRR type disease resistance protein S1472K I1474D >gb|ABF81413.1| TIR-NBS-LRR type disease resistance protein S630K I632D Solanum tuberosum (potatoes) >gb|AAP44390.1| nematode resistance protein [Solanum tuberosum] V655D Cucumis melo (Oriental melon) >gb|AAU04762.1| MRGH21 V675D Medicago sativa (alfalfa) >gb|ACF19651.1| TIR-NBS-LRR RCT1-like resistance protein I703D Populus balsamifera (balsam poplar) >gb|ABE99701.1| TIR-NBS-LRR disease resistance-like protein M689D Phaseolus vulgaris (French bean) >gb|ABH07384.1| CMR1 S653K V655D Glycine max (soybeans) >gb|AAO23067.1| R 12 protein E649K S651D >gb|AAO23066.1| R 3 protein E652K S654D >gb|AAO92748.1| candidate disease-resistance protein SR1 S653K S655D >gb|AAG09951.1| resistance protein LM6 E638K S640D Medicago truncatula >gb|ACF19650.1| TIR-NBS-LRR RCT1 resistance protein V678D >gb|ABD28507.1| Leucine-rich repeat; Leucine-rich E505K V507D Nicotiana tabacum (tobacco) >lcl|10469 gi|46577339|sp|Q40392.1| TMVRN_NICGU TMV resistance protein N E646K N648D Nicotiana glutinosa >sp|Q40392|TMVRN_NICGU TMV resistance protein N >gb|AAA50763.1| N Y646K N648D Solanum lycopersicum (tomato) >gb|AAR21295.1| bacterial spot disease resistance protein 4 Y682K N684D Solanum tuberosum subsp. andigena (patato) >emb|CAC82811.1| resistance gene-like Y655K G657D Lens culinaris (lentil) >emb|CAD56833.1| putative resistance gene analogue protein S756K V758D Linum usitatissimum (flax) >gb|AAK28809.1| AF310962_1 resistance-like protein P3-B E704K L708D >gb|AAK28806.1| AF310960_2 P2 rust resistance protein E719K L721D Vitis vinifera (wine grape) >emb|CAO24746.1| unnamed protein product I652D Oryza sativa Indica Group (Indian rice) >gb|EAY77148.1| hypothetical protein OsI_004995 H759K I761D Oryza sativa Japonica Group (Japanese rice) >gb|EAY84492.1| hypothetical protein OsI_005725 Y780K N782D 

1. An isolated nucleic acid molecule comprising a nucleotide sequence encoding a polypeptide comprising: (a) a nucleotide binding (NB) domain; and (b) a leucine rich repeat (LRR) domain, wherein said polypeptide confers a heat-stable defense response to a plant pathogen.
 2. The isolated nucleic acid molecule of claim 1, wherein said LRR domain includes a sub-domain that confers said heat stable defense response.
 3. The nucleic acid molecule of claim 1, wherein said nucleotide sequence is operably linked to a promoter that drives expression in a plant cell. 4-7. (canceled)
 8. The nucleic acid molecule of claim 1, wherein the LRR sub-domain that confers a heat-stable defense response to a plant pathogen includes an E/L(K or R)LD motif or an E/L(K or Y)LV(N or D) motif.
 9. The nucleic acid molecule of claim 1, wherein the polypeptide is SNC1-3, SNC1 E640R, N Y646K, or N Y646K N648D polypeptide.
 10. The nucleic acid molecule of claim 1, wherein the polypeptide is a homolog of SNC1, wherein said homolog includes said LRR sub-domain that confers a heat-stable defense response to a plant pathogen.
 11. The nucleic acid molecule of claim 1, wherein said polypeptide is described in FIG. 9, FIG. 10, or FIG.
 12. The nucleic acid molecule of claim 1, wherein the polypeptide is a homolog of N, wherein said homolog includes said LRR sub-domain that confers a heat-stable defense response to a plant pathogen.
 13. A vector comprising the nucleic acid molecule of claim
 1. 14. A cell comprising the nucleic acid molecule of claim
 1. 15. A plant or plant component comprising the nucleic acid molecule of claim
 1. 16. A method of conferring resistance to a pathogen in a plant or plant component, the method comprising the steps of: (a) transforming a plant cell with a nucleic acid molecule that encodes a polypeptide comprising: (i) a nucleotide binding (NB) domain; and (ii) a leucine rich repeat (LRR) domain, wherein said polypeptide confers a heat-stable defense response to a plant pathogen; and (b) regenerating a plant or plant component from said transformed plant cell, wherein said plant exhibits resistance to said pathogen.
 17. The method of claim 16, wherein said LRR domain includes a sub-domain that confers said heat stable defense response.
 18. The method of claim 16, wherein the plant or plant component expressing a heat-stable NB-LRR polypeptide has an increased level of resistance compared to a corresponding control plant at the masking temperature of the control plant or control plant component.
 19. The method of claim 16, wherein said nucleotide sequence is operably linked to a promoter that drives expression in a plant cell. 20-23. (canceled)
 24. The method of claim 16, wherein the LRR sub-domain that confers a heat-stable defense response to a plant pathogen includes an EL(K or R)LD motif or an EL(K or Y)LV(N or D) motif. 25-26. (canceled)
 27. The method of claim 16, wherein said plant or plant component is a monocot or a dicot.
 28. The method of claim 16, wherein said pathogen is a bacterial, a insect, a nematode, a fungal, or a viral pathogen. 29-36. (canceled)
 37. A plant or plant component comprising a substantially-pure polypeptide comprising: (a) a nucleotide binding (NB) domain; and (b) a leucine rich repeat (LRR) domain, wherein said polypeptide confers a heat-stable defense response to a plant pathogen.
 38. The plant or plant component of claim 37, wherein said LRR domain includes a sub-domain that confers said heat stable defense response. 39-40. (canceled) 